CA2507117A1 - Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines - Google Patents

Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines Download PDF

Info

Publication number: CA2507117A1
Authority: CA; Canada
Prior art keywords: protein; chip; proteins; chemical; sample
Prior art date: 2005-05-11
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.): Abandoned

Application number

CA 2507117

Other languages

English (en)

Inventor

Bernard F. Gibbs

Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)

Individual

Original Assignee

Individual

Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)

2005-05-11

Filing date

2005-05-11

Publication date

2006-11-11

2005-05-11 Application filed by Individual filed Critical Individual

2005-05-11 Priority to CA 2507117 priority Critical patent/CA2507117A1/fr

2006-05-11 Priority to US11/431,820 priority patent/US7622273B2/en

2006-11-11 Publication of CA2507117A1 publication Critical patent/CA2507117A1/fr

Status Abandoned legal-status Critical Current

Links

108090000623 proteins and genes Proteins 0.000 title claims abstract description 237
102000004169 proteins and genes Human genes 0.000 title claims abstract description 236
239000000126 substance Substances 0.000 title claims abstract description 45
230000002255 enzymatic effect Effects 0.000 title claims description 34
238000011282 treatment Methods 0.000 title abstract description 28
238000003491 array Methods 0.000 title abstract description 8
108091005608 glycosylated proteins Proteins 0.000 title description 2
102000035122 glycosylated proteins Human genes 0.000 title description 2
108091005981 phosphorylated proteins Proteins 0.000 title description 2
238000000034 method Methods 0.000 claims abstract description 99
108090000765 processed proteins & peptides Proteins 0.000 claims abstract description 51
238000004458 analytical method Methods 0.000 claims abstract description 46
102000004196 processed proteins & peptides Human genes 0.000 claims abstract description 43
230000022811 deglycosylation Effects 0.000 claims abstract description 37
238000006243 chemical reaction Methods 0.000 claims abstract description 35
230000029087 digestion Effects 0.000 claims abstract description 25
230000030609 dephosphorylation Effects 0.000 claims abstract description 24
238000006209 dephosphorylation reaction Methods 0.000 claims abstract description 24
230000029936 alkylation Effects 0.000 claims abstract description 18
238000005804 alkylation reaction Methods 0.000 claims abstract description 18
238000000955 peptide mass fingerprinting Methods 0.000 claims abstract description 18
230000009467 reduction Effects 0.000 claims abstract description 16
230000036425 denaturation Effects 0.000 claims abstract description 15
238000004925 denaturation Methods 0.000 claims abstract description 15
239000000523 sample Substances 0.000 claims description 69
238000004949 mass spectrometry Methods 0.000 claims description 47
102000004190 Enzymes Human genes 0.000 claims description 14
108090000790 Enzymes Proteins 0.000 claims description 14
238000003795 desorption Methods 0.000 claims description 11
230000002452 interceptive effect Effects 0.000 claims description 10
230000003750 conditioning effect Effects 0.000 claims description 9
238000004587 chromatography analysis Methods 0.000 claims description 7
238000011068 loading method Methods 0.000 claims description 7
230000002441 reversible effect Effects 0.000 claims description 5
239000003446 ligand Substances 0.000 claims description 4
238000005342 ion exchange Methods 0.000 claims description 3
102000005962 receptors Human genes 0.000 claims description 3
108020003175 receptors Proteins 0.000 claims description 3
238000005406 washing Methods 0.000 claims description 3
102000004856 Lectins Human genes 0.000 claims description 2
108090001090 Lectins Proteins 0.000 claims description 2
PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 claims description 2
239000010931 gold Substances 0.000 claims description 2
229910052737 gold Inorganic materials 0.000 claims description 2
239000002523 lectin Substances 0.000 claims description 2
239000012521 purified sample Substances 0.000 claims 1
238000006722 reduction reaction Methods 0.000 abstract description 17
239000012472 biological sample Substances 0.000 abstract description 13
230000006862 enzymatic digestion Effects 0.000 abstract description 13
238000012512 characterization method Methods 0.000 abstract description 10
210000002700 urine Anatomy 0.000 abstract description 10
102000035195 Peptidases Human genes 0.000 abstract description 7
108091005804 Peptidases Proteins 0.000 abstract description 7
239000004365 Protease Substances 0.000 abstract description 6
239000000090 biomarker Substances 0.000 abstract description 4
235000018102 proteins Nutrition 0.000 description 215
108010058846 Ovalbumin Proteins 0.000 description 23
229940092253 ovalbumin Drugs 0.000 description 23
239000000243 solution Substances 0.000 description 21
108060002885 fetuin Proteins 0.000 description 17
102000013361 fetuin Human genes 0.000 description 17
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 16
230000027455 binding Effects 0.000 description 15
230000013595 glycosylation Effects 0.000 description 15
150000002500 ions Chemical class 0.000 description 14
108090000631 Trypsin Proteins 0.000 description 13
102000004142 Trypsin Human genes 0.000 description 13
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 13
238000005516 engineering process Methods 0.000 description 13
229940088598 enzyme Drugs 0.000 description 13
230000002209 hydrophobic effect Effects 0.000 description 13
239000012588 trypsin Substances 0.000 description 13
239000000872 buffer Substances 0.000 description 12
239000003153 chemical reaction reagent Substances 0.000 description 12
238000006206 glycosylation reaction Methods 0.000 description 12
230000002829 reductive effect Effects 0.000 description 12
238000013459 approach Methods 0.000 description 11
230000003993 interaction Effects 0.000 description 11
239000011159 matrix material Substances 0.000 description 11
239000012071 phase Substances 0.000 description 10
238000006366 phosphorylation reaction Methods 0.000 description 10
230000017854 proteolysis Effects 0.000 description 10
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 9
150000001413 amino acids Chemical class 0.000 description 9
239000003599 detergent Substances 0.000 description 9
238000000816 matrix-assisted laser desorption--ionisation Methods 0.000 description 9
239000000203 mixture Substances 0.000 description 9
230000026731 phosphorylation Effects 0.000 description 9
150000003839 salts Chemical class 0.000 description 9
PCMORTLOPMLEFB-ONEGZZNKSA-N sinapic acid Chemical class COC1=CC(\C=C\C(O)=O)=CC(OC)=C1O PCMORTLOPMLEFB-ONEGZZNKSA-N 0.000 description 9
235000000346 sugar Nutrition 0.000 description 9
IAZDPXIOMUYVGZ-UHFFFAOYSA-N Dimethylsulphoxide Chemical compound CS(C)=O IAZDPXIOMUYVGZ-UHFFFAOYSA-N 0.000 description 8
102000003886 Glycoproteins Human genes 0.000 description 8
108090000288 Glycoproteins Proteins 0.000 description 8
101001018085 Lysobacter enzymogenes Lysyl endopeptidase Proteins 0.000 description 8
108010055817 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Proteins 0.000 description 8
102000000447 Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase Human genes 0.000 description 8
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 8
235000001014 amino acid Nutrition 0.000 description 8
229940024606 amino acid Drugs 0.000 description 8
210000004027 cell Anatomy 0.000 description 8
239000000758 substrate Substances 0.000 description 8
102000001301 EGF receptor Human genes 0.000 description 7
108060006698 EGF receptor Proteins 0.000 description 7
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 7
241000700159 Rattus Species 0.000 description 7
108010018360 alpha 2u globulin Proteins 0.000 description 7
239000012491 analyte Substances 0.000 description 7
150000001875 compounds Chemical class 0.000 description 7
239000012634 fragment Substances 0.000 description 7
238000001819 mass spectrum Methods 0.000 description 7
230000035484 reaction time Effects 0.000 description 7
102000005348 Neuraminidase Human genes 0.000 description 6
108010006232 Neuraminidase Proteins 0.000 description 6
230000002152 alkylating effect Effects 0.000 description 6
239000003638 chemical reducing agent Substances 0.000 description 6
238000011161 development Methods 0.000 description 6
201000010099 disease Diseases 0.000 description 6
208000037265 diseases, disorders, signs and symptoms Diseases 0.000 description 6
238000006911 enzymatic reaction Methods 0.000 description 6
229920001184 polypeptide Polymers 0.000 description 6
230000008569 process Effects 0.000 description 6
230000009822 protein phosphorylation Effects 0.000 description 6
230000035945 sensitivity Effects 0.000 description 6
PCMORTLOPMLEFB-UHFFFAOYSA-N sinapinic acid Natural products COC1=CC(C=CC(O)=O)=CC(OC)=C1O PCMORTLOPMLEFB-UHFFFAOYSA-N 0.000 description 6
-1 Glu-C endoproteinase Proteins 0.000 description 5
206010028980 Neoplasm Diseases 0.000 description 5
239000002253 acid Substances 0.000 description 5
239000002168 alkylating agent Substances 0.000 description 5
229940100198 alkylating agent Drugs 0.000 description 5
230000004888 barrier function Effects 0.000 description 5
150000001720 carbohydrates Chemical class 0.000 description 5
238000003776 cleavage reaction Methods 0.000 description 5
239000011248 coating agent Substances 0.000 description 5
238000000576 coating method Methods 0.000 description 5
238000001514 detection method Methods 0.000 description 5
238000002474 experimental method Methods 0.000 description 5
230000006870 function Effects 0.000 description 5
239000007789 gas Substances 0.000 description 5
230000004048 modification Effects 0.000 description 5
238000012986 modification Methods 0.000 description 5
150000002482 oligosaccharides Chemical class 0.000 description 5
230000004481 post-translational protein modification Effects 0.000 description 5
230000002797 proteolythic effect Effects 0.000 description 5
230000007017 scission Effects 0.000 description 5
239000007787 solid Substances 0.000 description 5
238000000672 surface-enhanced laser desorption--ionisation Methods 0.000 description 5
230000002485 urinary effect Effects 0.000 description 5
241000283690 Bos taurus Species 0.000 description 4
108020004414 DNA Proteins 0.000 description 4
101000609762 Gallus gallus Ovalbumin Proteins 0.000 description 4
230000004988 N-glycosylation Effects 0.000 description 4
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 4
201000011510 cancer Diseases 0.000 description 4
239000004202 carbamide Substances 0.000 description 4
235000014633 carbohydrates Nutrition 0.000 description 4
HJMZMZRCABDKKV-UHFFFAOYSA-N carbonocyanidic acid Chemical compound OC(=O)C#N HJMZMZRCABDKKV-UHFFFAOYSA-N 0.000 description 4
238000000126 in silico method Methods 0.000 description 4
230000002401 inhibitory effect Effects 0.000 description 4
PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 4
238000001698 laser desorption ionisation Methods 0.000 description 4
239000007788 liquid Substances 0.000 description 4
230000009145 protein modification Effects 0.000 description 4
238000011160 research Methods 0.000 description 4
230000000717 retained effect Effects 0.000 description 4
WXTMDXOMEHJXQO-UHFFFAOYSA-N 2,5-dihydroxybenzoic acid Chemical compound OC(=O)C1=CC(O)=CC=C1O WXTMDXOMEHJXQO-UHFFFAOYSA-N 0.000 description 3
239000000275 Adrenocorticotropic Hormone Substances 0.000 description 3
102000002260 Alkaline Phosphatase Human genes 0.000 description 3
108020004774 Alkaline Phosphatase Proteins 0.000 description 3
ATRRKUHOCOJYRX-UHFFFAOYSA-N Ammonium bicarbonate Chemical compound [NH4+].OC([O-])=O ATRRKUHOCOJYRX-UHFFFAOYSA-N 0.000 description 3
229910000013 Ammonium bicarbonate Inorganic materials 0.000 description 3
101001011741 Bos taurus Insulin Proteins 0.000 description 3
102100021935 C-C motif chemokine 26 Human genes 0.000 description 3
102400000739 Corticotropin Human genes 0.000 description 3
101800000414 Corticotropin Proteins 0.000 description 3
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 3
PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 3
101000897493 Homo sapiens C-C motif chemokine 26 Proteins 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
ZMXDDKWLCZADIW-UHFFFAOYSA-N N,N-Dimethylformamide Chemical compound CN(C)C=O ZMXDDKWLCZADIW-UHFFFAOYSA-N 0.000 description 3
102100031119 Parvalbumin alpha Human genes 0.000 description 3
101710180659 Parvalbumin alpha Proteins 0.000 description 3
235000012538 ammonium bicarbonate Nutrition 0.000 description 3
239000001099 ammonium carbonate Substances 0.000 description 3
238000005349 anion exchange Methods 0.000 description 3
230000008901 benefit Effects 0.000 description 3
239000012148 binding buffer Substances 0.000 description 3
230000015572 biosynthetic process Effects 0.000 description 3
IXIBAKNTJSCKJM-BUBXBXGNSA-N bovine insulin Chemical compound C([C@@H](C(=O)N[C@@H](CC(C)C)C(=O)N[C@H]1CSSC[C@H]2C(=O)N[C@@H](C)C(=O)N[C@@H](CO)C(=O)N[C@H](C(=O)N[C@H](C(N[C@@H](CO)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(N)=O)C(=O)N[C@@H](CC=3C=CC(O)=CC=3)C(=O)N[C@@H](CSSC[C@H](NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3C=CC(O)=CC=3)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](C)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC=3NC=NC=3)NC(=O)[C@H](CO)NC(=O)CNC1=O)C(=O)NCC(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CCCNC(N)=N)C(=O)NCC(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N[C@@H]([C@@H](C)O)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C)C(O)=O)C(=O)N[C@@H](CC(N)=O)C(O)=O)=O)CSSC[C@@H](C(N2)=O)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@H](C(C)C)NC(=O)[C@@H](NC(=O)CN)[C@@H](C)CC)C(C)C)NC(=O)[C@H](CCC(N)=O)NC(=O)[C@H](CC(N)=O)NC(=O)[C@@H](NC(=O)[C@@H](N)CC=1C=CC=CC=1)C(C)C)C1=CN=CN1 IXIBAKNTJSCKJM-BUBXBXGNSA-N 0.000 description 3
230000015556 catabolic process Effects 0.000 description 3
210000001175 cerebrospinal fluid Anatomy 0.000 description 3
238000007385 chemical modification Methods 0.000 description 3
150000001851 cinnamic acid derivatives Chemical class 0.000 description 3
IDLFZVILOHSSID-OVLDLUHVSA-N corticotropin Chemical compound C([C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H](CCSC)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1NC=NC=1)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC=1C2=CC=CC=C2NC=1)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)NCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](C(C)C)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CO)C(=O)N[C@@H](C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](C)C(=O)N[C@@H](CC=1C=CC=CC=1)C(=O)N1[C@@H](CCC1)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(=O)N[C@@H](CC=1C=CC=CC=1)C(O)=O)NC(=O)[C@@H](N)CO)C1=CC=C(O)C=C1 IDLFZVILOHSSID-OVLDLUHVSA-N 0.000 description 3
229960000258 corticotropin Drugs 0.000 description 3
239000013078 crystal Substances 0.000 description 3
ATDGTVJJHBUTRL-UHFFFAOYSA-N cyanogen bromide Chemical compound BrC#N ATDGTVJJHBUTRL-UHFFFAOYSA-N 0.000 description 3
230000003247 decreasing effect Effects 0.000 description 3
238000006731 degradation reaction Methods 0.000 description 3
230000001419 dependent effect Effects 0.000 description 3
239000003814 drug Substances 0.000 description 3
238000000132 electrospray ionisation Methods 0.000 description 3
238000005194 fractionation Methods 0.000 description 3
150000004676 glycans Chemical group 0.000 description 3
230000014759 maintenance of location Effects 0.000 description 3
239000000463 material Substances 0.000 description 3
229920001542 oligosaccharide Polymers 0.000 description 3
201000001474 proteinuria Diseases 0.000 description 3
JUJWROOIHBZHMG-UHFFFAOYSA-N pyridine Substances C1=CC=NC=C1 JUJWROOIHBZHMG-UHFFFAOYSA-N 0.000 description 3
239000012465 retentate Substances 0.000 description 3
238000000926 separation method Methods 0.000 description 3
FVAUCKIRQBBSSJ-UHFFFAOYSA-M sodium iodide Chemical compound [Na+].[I-] FVAUCKIRQBBSSJ-UHFFFAOYSA-M 0.000 description 3
150000008163 sugars Chemical class 0.000 description 3
238000004885 tandem mass spectrometry Methods 0.000 description 3
238000001269 time-of-flight mass spectrometry Methods 0.000 description 3
210000001519 tissue Anatomy 0.000 description 3
239000011534 wash buffer Substances 0.000 description 3
YBJHBAHKTGYVGT-ZKWXMUAHSA-N (+)-Biotin Chemical group N1C(=O)N[C@@H]2[C@H](CCCCC(=O)O)SC[C@@H]21 YBJHBAHKTGYVGT-ZKWXMUAHSA-N 0.000 description 2
XJODGRWDFZVTKW-LURJTMIESA-N (2s)-4-methyl-2-(methylamino)pentanoic acid Chemical compound CN[C@H](C(O)=O)CC(C)C XJODGRWDFZVTKW-LURJTMIESA-N 0.000 description 2
FUOOLUPWFVMBKG-UHFFFAOYSA-N 2-Aminoisobutyric acid Chemical compound CC(C)(N)C(O)=O FUOOLUPWFVMBKG-UHFFFAOYSA-N 0.000 description 2
NQUNIMFHIWQQGJ-UHFFFAOYSA-N 2-nitro-5-thiocyanatobenzoic acid Chemical compound OC(=O)C1=CC(SC#N)=CC=C1[N+]([O-])=O NQUNIMFHIWQQGJ-UHFFFAOYSA-N 0.000 description 2
KEJYUAMBFQZVEH-UHFFFAOYSA-N 3-cyano-2-hydroxy-3-phenylprop-2-enoic acid Chemical compound OC(=O)C(O)=C(C#N)C1=CC=CC=C1 KEJYUAMBFQZVEH-UHFFFAOYSA-N 0.000 description 2
RYSMHWILUNYBFW-UHFFFAOYSA-N 4-amino-2-[6-(dimethylamino)purin-9-yl]-5-(hydroxymethyl)oxolan-3-ol Chemical compound C1=NC=2C(N(C)C)=NC=NC=2N1C1OC(CO)C(N)C1O RYSMHWILUNYBFW-UHFFFAOYSA-N 0.000 description 2
RZVAJINKPMORJF-UHFFFAOYSA-N Acetaminophen Chemical compound CC(=O)NC1=CC=C(O)C=C1 RZVAJINKPMORJF-UHFFFAOYSA-N 0.000 description 2
HRPVXLWXLXDGHG-UHFFFAOYSA-N Acrylamide Chemical compound NC(=O)C=C HRPVXLWXLXDGHG-UHFFFAOYSA-N 0.000 description 2
102000009027 Albumins Human genes 0.000 description 2
108010088751 Albumins Proteins 0.000 description 2
208000035404 Autolysis Diseases 0.000 description 2
108091003079 Bovine Serum Albumin Proteins 0.000 description 2
206010057248 Cell death Diseases 0.000 description 2
101000726354 Equus caballus Cytochrome c Proteins 0.000 description 2
ZHNUHDYFZUAESO-UHFFFAOYSA-N Formamide Chemical compound NC=O ZHNUHDYFZUAESO-UHFFFAOYSA-N 0.000 description 2
241000287828 Gallus gallus Species 0.000 description 2
108010051815 Glutamyl endopeptidase Proteins 0.000 description 2
ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
101000971703 Homo sapiens Kinesin-like protein KIF1C Proteins 0.000 description 2
101000979579 Homo sapiens NK1 transcription factor-related protein 1 Proteins 0.000 description 2
102100021525 Kinesin-like protein KIF1C Human genes 0.000 description 2
TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 2
102000016943 Muramidase Human genes 0.000 description 2
108010014251 Muramidase Proteins 0.000 description 2
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 2
PCLIMKBDDGJMGD-UHFFFAOYSA-N N-bromosuccinimide Chemical compound BrN1C(=O)CCC1=O PCLIMKBDDGJMGD-UHFFFAOYSA-N 0.000 description 2
JRNVZBWKYDBUCA-UHFFFAOYSA-N N-chlorosuccinimide Chemical compound ClN1C(=O)CCC1=O JRNVZBWKYDBUCA-UHFFFAOYSA-N 0.000 description 2
GDFAOVXKHJXLEI-VKHMYHEASA-N N-methyl-L-alanine Chemical compound C[NH2+][C@@H](C)C([O-])=O GDFAOVXKHJXLEI-VKHMYHEASA-N 0.000 description 2
230000004989 O-glycosylation Effects 0.000 description 2
206010033128 Ovarian cancer Diseases 0.000 description 2
206010061535 Ovarian neoplasm Diseases 0.000 description 2
229910019142 PO4 Inorganic materials 0.000 description 2
ISWSIDIOOBJBQZ-UHFFFAOYSA-N Phenol Chemical compound OC1=CC=CC=C1 ISWSIDIOOBJBQZ-UHFFFAOYSA-N 0.000 description 2
102000007982 Phosphoproteins Human genes 0.000 description 2
108010089430 Phosphoproteins Proteins 0.000 description 2
102000004160 Phosphoric Monoester Hydrolases Human genes 0.000 description 2
108090000608 Phosphoric Monoester Hydrolases Proteins 0.000 description 2
239000002202 Polyethylene glycol Substances 0.000 description 2
102100030350 Prolactin-inducible protein Human genes 0.000 description 2
101710088644 Prolactin-inducible protein Proteins 0.000 description 2
108010026552 Proteome Proteins 0.000 description 2
DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical compound [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 description 2
AYFVYJQAPQTCCC-UHFFFAOYSA-N Threonine Natural products CC(O)C(N)C(O)=O AYFVYJQAPQTCCC-UHFFFAOYSA-N 0.000 description 2
239000004473 Threonine Substances 0.000 description 2
230000002159 abnormal effect Effects 0.000 description 2
238000005903 acid hydrolysis reaction Methods 0.000 description 2
150000001412 amines Chemical group 0.000 description 2
239000000427 antigen Substances 0.000 description 2
239000007864 aqueous solution Substances 0.000 description 2
238000005842 biochemical reaction Methods 0.000 description 2
229940098773 bovine serum albumin Drugs 0.000 description 2
150000007942 carboxylates Chemical group 0.000 description 2
239000013043 chemical agent Substances 0.000 description 2
238000013375 chromatographic separation Methods 0.000 description 2
230000000295 complement effect Effects 0.000 description 2
230000001143 conditioned effect Effects 0.000 description 2
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 2
FFYPMLJYZAEMQB-UHFFFAOYSA-N diethyl pyrocarbonate Chemical compound CCOC(=O)OC(=O)OCC FFYPMLJYZAEMQB-UHFFFAOYSA-N 0.000 description 2
229940079593 drug Drugs 0.000 description 2
230000000694 effects Effects 0.000 description 2
239000000796 flavoring agent Substances 0.000 description 2
235000019634 flavors Nutrition 0.000 description 2
230000007062 hydrolysis Effects 0.000 description 2
238000006460 hydrolysis reaction Methods 0.000 description 2
238000011534 incubation Methods 0.000 description 2
NOESYZHRGYRDHS-UHFFFAOYSA-N insulin Chemical compound N1C(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(NC(=O)CN)C(C)CC)CSSCC(C(NC(CO)C(=O)NC(CC(C)C)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CCC(N)=O)C(=O)NC(CC(C)C)C(=O)NC(CCC(O)=O)C(=O)NC(CC(N)=O)C(=O)NC(CC=2C=CC(O)=CC=2)C(=O)NC(CSSCC(NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2C=CC(O)=CC=2)NC(=O)C(CC(C)C)NC(=O)C(C)NC(=O)C(CCC(O)=O)NC(=O)C(C(C)C)NC(=O)C(CC(C)C)NC(=O)C(CC=2NC=NC=2)NC(=O)C(CO)NC(=O)CNC2=O)C(=O)NCC(=O)NC(CCC(O)=O)C(=O)NC(CCCNC(N)=N)C(=O)NCC(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC=CC=3)C(=O)NC(CC=3C=CC(O)=CC=3)C(=O)NC(C(C)O)C(=O)N3C(CCC3)C(=O)NC(CCCCN)C(=O)NC(C)C(O)=O)C(=O)NC(CC(N)=O)C(O)=O)=O)NC(=O)C(C(C)CC)NC(=O)C(CO)NC(=O)C(C(C)O)NC(=O)C1CSSCC2NC(=O)C(CC(C)C)NC(=O)C(NC(=O)C(CCC(N)=O)NC(=O)C(CC(N)=O)NC(=O)C(NC(=O)C(N)CC=1C=CC=CC=1)C(C)C)CC1=CN=CN1 NOESYZHRGYRDHS-UHFFFAOYSA-N 0.000 description 2
238000011835 investigation Methods 0.000 description 2
238000002955 isolation Methods 0.000 description 2
JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
230000000670 limiting effect Effects 0.000 description 2
AMXOYNBUYSYVKV-UHFFFAOYSA-M lithium bromide Chemical compound [Li+].[Br-] AMXOYNBUYSYVKV-UHFFFAOYSA-M 0.000 description 2
229960000274 lysozyme Drugs 0.000 description 2
239000004325 lysozyme Substances 0.000 description 2
235000010335 lysozyme Nutrition 0.000 description 2
BDAGIHXWWSANSR-UHFFFAOYSA-N methanoic acid Natural products OC=O BDAGIHXWWSANSR-UHFFFAOYSA-N 0.000 description 2
102000035118 modified proteins Human genes 0.000 description 2
108091005573 modified proteins Proteins 0.000 description 2
238000012544 monitoring process Methods 0.000 description 2
108020004707 nucleic acids Proteins 0.000 description 2
102000039446 nucleic acids Human genes 0.000 description 2
150000007523 nucleic acids Chemical class 0.000 description 2
239000003960 organic solvent Substances 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-K phosphate Chemical compound [O-]P([O-])([O-])=O NBIIXXVUZAFLBC-UHFFFAOYSA-K 0.000 description 2
239000010452 phosphate Substances 0.000 description 2
125000002467 phosphate group Chemical group [H]OP(=O)(O[H])O[*] 0.000 description 2
BZQFBWGGLXLEPQ-REOHCLBHSA-N phosphoserine Chemical compound OC(=O)[C@@H](N)COP(O)(O)=O BZQFBWGGLXLEPQ-REOHCLBHSA-N 0.000 description 2
210000002381 plasma Anatomy 0.000 description 2
229920001223 polyethylene glycol Polymers 0.000 description 2
230000001323 posttranslational effect Effects 0.000 description 2
239000000047 product Substances 0.000 description 2
235000019833 protease Nutrition 0.000 description 2
238000000746 purification Methods 0.000 description 2
RXWNCPJZOCPEPQ-NVWDDTSBSA-N puromycin Chemical compound C1=CC(OC)=CC=C1C[C@H](N)C(=O)N[C@H]1[C@@H](O)[C@H](N2C3=NC=NC(=C3N=C2)N(C)C)O[C@@H]1CO RXWNCPJZOCPEPQ-NVWDDTSBSA-N 0.000 description 2
230000001105 regulatory effect Effects 0.000 description 2
238000004366 reverse phase liquid chromatography Methods 0.000 description 2
238000004007 reversed phase HPLC Methods 0.000 description 2
230000028043 self proteolysis Effects 0.000 description 2
238000012163 sequencing technique Methods 0.000 description 2
235000019333 sodium laurylsulphate Nutrition 0.000 description 2
238000012360 testing method Methods 0.000 description 2
WROMPOXWARCANT-UHFFFAOYSA-N tfa trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F.OC(=O)C(F)(F)F WROMPOXWARCANT-UHFFFAOYSA-N 0.000 description 2
CWERGRDVMFNCDR-UHFFFAOYSA-N thioglycolic acid Chemical compound OC(=O)CS CWERGRDVMFNCDR-UHFFFAOYSA-N 0.000 description 2
238000012784 weak cation exchange Methods 0.000 description 2
FDKWRPBBCBCIGA-REOHCLBHSA-N (2r)-2-azaniumyl-3-$l^{1}-selanylpropanoate Chemical compound [Se]C[C@H](N)C(O)=O FDKWRPBBCBCIGA-REOHCLBHSA-N 0.000 description 1
OJKODEIWYUKXIM-PFSAKTOKSA-N (e,2s,3r,4r)-3-hydroxy-4-methyl-2-(methylamino)oct-5-enoic acid Chemical compound CC\C=C\[C@@H](C)[C@@H](O)[C@H](NC)C(O)=O OJKODEIWYUKXIM-PFSAKTOKSA-N 0.000 description 1
AHQFCPOIMVMDEZ-UNISNWAASA-N (e,2s,3r,4r)-3-hydroxy-4-methyl-2-(methylamino)oct-6-enoic acid Chemical compound CN[C@H](C(O)=O)[C@H](O)[C@H](C)C\C=C\C AHQFCPOIMVMDEZ-UNISNWAASA-N 0.000 description 1
WBYWAXJHAXSJNI-VOTSOKGWSA-M .beta-Phenylacrylic acid Natural products [O-]C(=O)\C=C\C1=CC=CC=C1 WBYWAXJHAXSJNI-VOTSOKGWSA-M 0.000 description 1
LRMSQVBRUNSOJL-UHFFFAOYSA-N 2,2,3,3,3-pentafluoropropanoic acid Chemical compound OC(=O)C(F)(F)C(F)(F)F LRMSQVBRUNSOJL-UHFFFAOYSA-N 0.000 description 1
IXDMCRDIEUXFAU-UHFFFAOYSA-N 2-(tribromomethyl)phenol Chemical compound OC1=CC=CC=C1C(Br)(Br)Br IXDMCRDIEUXFAU-UHFFFAOYSA-N 0.000 description 1
DJQYYYCQOZMCRC-UHFFFAOYSA-N 2-aminopropane-1,3-dithiol Chemical compound SCC(N)CS DJQYYYCQOZMCRC-UHFFFAOYSA-N 0.000 description 1
OSWFIVFLDKOXQC-UHFFFAOYSA-N 4-(3-methoxyphenyl)aniline Chemical compound COC1=CC=CC(C=2C=CC(N)=CC=2)=C1 OSWFIVFLDKOXQC-UHFFFAOYSA-N 0.000 description 1
KFDVPJUYSDEJTH-UHFFFAOYSA-N 4-ethenylpyridine Chemical compound C=CC1=CC=NC=C1 KFDVPJUYSDEJTH-UHFFFAOYSA-N 0.000 description 1
102100022749 Aminopeptidase N Human genes 0.000 description 1
YNSCBOUZTAGIGO-ZLUOBGJFSA-N Asn-Asn-Cys Chemical compound C([C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](CS)C(=O)O)N)C(=O)N YNSCBOUZTAGIGO-ZLUOBGJFSA-N 0.000 description 1
DCXYFEDJOCDNAF-UHFFFAOYSA-N Asparagine Natural products OC(=O)C(N)CC(N)=O DCXYFEDJOCDNAF-UHFFFAOYSA-N 0.000 description 1
208000023275 Autoimmune disease Diseases 0.000 description 1
NOWKCMXCCJGMRR-UHFFFAOYSA-N Aziridine Chemical compound C1CN1 NOWKCMXCCJGMRR-UHFFFAOYSA-N 0.000 description 1
BXTVQNYQYUTQAZ-UHFFFAOYSA-N BNPS-skatole Chemical compound N=1C2=CC=CC=C2C(C)(Br)C=1SC1=CC=CC=C1[N+]([O-])=O BXTVQNYQYUTQAZ-UHFFFAOYSA-N 0.000 description 1
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
238000009010 Bradford assay Methods 0.000 description 1
206010006187 Breast cancer Diseases 0.000 description 1
208000026310 Breast neoplasm Diseases 0.000 description 1
108010049990 CD13 Antigens Proteins 0.000 description 1
108090000087 Carboxypeptidase B Proteins 0.000 description 1
102000003670 Carboxypeptidase B Human genes 0.000 description 1
108010080937 Carboxypeptidases A Proteins 0.000 description 1
102000000496 Carboxypeptidases A Human genes 0.000 description 1
208000024172 Cardiovascular disease Diseases 0.000 description 1
102000014914 Carrier Proteins Human genes 0.000 description 1
108010076667 Caspases Proteins 0.000 description 1
102000011727 Caspases Human genes 0.000 description 1
108010059081 Cathepsin A Proteins 0.000 description 1
102000005572 Cathepsin A Human genes 0.000 description 1
108090000317 Chymotrypsin Proteins 0.000 description 1
108091035707 Consensus sequence Proteins 0.000 description 1
FDKWRPBBCBCIGA-UWTATZPHSA-N D-Selenocysteine Natural products [Se]C[C@@H](N)C(O)=O FDKWRPBBCBCIGA-UWTATZPHSA-N 0.000 description 1
150000008574 D-amino acids Chemical class 0.000 description 1
102000053602 DNA Human genes 0.000 description 1
102000052510 DNA-Binding Proteins Human genes 0.000 description 1
101710096438 DNA-binding protein Proteins 0.000 description 1
BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
108010067770 Endopeptidase K Proteins 0.000 description 1
102000005593 Endopeptidases Human genes 0.000 description 1
108010059378 Endopeptidases Proteins 0.000 description 1
108010013369 Enteropeptidase Proteins 0.000 description 1
102100029727 Enteropeptidase Human genes 0.000 description 1
108010074860 Factor Xa Proteins 0.000 description 1
108010024636 Glutathione Proteins 0.000 description 1
108010031186 Glycoside Hydrolases Proteins 0.000 description 1
102000005744 Glycoside Hydrolases Human genes 0.000 description 1
101000882911 Hathewaya histolytica Clostripain Proteins 0.000 description 1
CPELXLSAUQHCOX-UHFFFAOYSA-N Hydrogen bromide Chemical compound Br CPELXLSAUQHCOX-UHFFFAOYSA-N 0.000 description 1
AVXURJPOCDRRFD-UHFFFAOYSA-N Hydroxylamine Chemical compound ON AVXURJPOCDRRFD-UHFFFAOYSA-N 0.000 description 1
108090001061 Insulin Proteins 0.000 description 1
102000004877 Insulin Human genes 0.000 description 1
102000011782 Keratins Human genes 0.000 description 1
108010076876 Keratins Proteins 0.000 description 1
SNDPXSYFESPGGJ-BYPYZUCNSA-N L-2-aminopentanoic acid Chemical compound CCC[C@H](N)C(O)=O SNDPXSYFESPGGJ-BYPYZUCNSA-N 0.000 description 1
AHLPHDHHMVZTML-BYPYZUCNSA-N L-Ornithine Chemical compound NCCC[C@H](N)C(O)=O AHLPHDHHMVZTML-BYPYZUCNSA-N 0.000 description 1
DCXYFEDJOCDNAF-REOHCLBHSA-N L-asparagine Chemical compound OC(=O)[C@@H](N)CC(N)=O DCXYFEDJOCDNAF-REOHCLBHSA-N 0.000 description 1
RHGKLRLOHDJJDR-BYPYZUCNSA-N L-citrulline Chemical compound NC(=O)NCCC[C@H]([NH3+])C([O-])=O RHGKLRLOHDJJDR-BYPYZUCNSA-N 0.000 description 1
ZDXPYRJPNDTMRX-VKHMYHEASA-N L-glutamine Chemical compound OC(=O)[C@@H](N)CCC(N)=O ZDXPYRJPNDTMRX-VKHMYHEASA-N 0.000 description 1
SNDPXSYFESPGGJ-UHFFFAOYSA-N L-norVal-OH Natural products CCCC(N)C(O)=O SNDPXSYFESPGGJ-UHFFFAOYSA-N 0.000 description 1
AYFVYJQAPQTCCC-GBXIJSLDSA-N L-threonine Chemical compound C[C@@H](O)[C@H](N)C(O)=O AYFVYJQAPQTCCC-GBXIJSLDSA-N 0.000 description 1
239000002841 Lewis acid Substances 0.000 description 1
239000002879 Lewis base Substances 0.000 description 1
108010090665 Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase Proteins 0.000 description 1
102000007474 Multiprotein Complexes Human genes 0.000 description 1
108010085220 Multiprotein Complexes Proteins 0.000 description 1
SQVRNKJHWKZAKO-PFQGKNLYSA-N N-acetyl-beta-neuraminic acid Chemical compound CC(=O)N[C@@H]1[C@@H](O)C[C@@](O)(C(O)=O)O[C@H]1[C@H](O)[C@H](O)CO SQVRNKJHWKZAKO-PFQGKNLYSA-N 0.000 description 1
CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
RHGKLRLOHDJJDR-UHFFFAOYSA-N Ndelta-carbamoyl-DL-ornithine Natural products OC(=O)C(N)CCCNC(N)=O RHGKLRLOHDJJDR-UHFFFAOYSA-N 0.000 description 1
BZQFBWGGLXLEPQ-UHFFFAOYSA-N O-phosphoryl-L-serine Natural products OC(=O)C(N)COP(O)(O)=O BZQFBWGGLXLEPQ-UHFFFAOYSA-N 0.000 description 1
AHLPHDHHMVZTML-UHFFFAOYSA-N Orn-delta-NH2 Natural products NCCCC(N)C(O)=O AHLPHDHHMVZTML-UHFFFAOYSA-N 0.000 description 1
UTJLXEIPEHZYQJ-UHFFFAOYSA-N Ornithine Natural products OC(=O)C(C)CCCN UTJLXEIPEHZYQJ-UHFFFAOYSA-N 0.000 description 1
BPQQTUXANYXVAA-UHFFFAOYSA-N Orthosilicate Chemical group [O-][Si]([O-])([O-])[O-] BPQQTUXANYXVAA-UHFFFAOYSA-N 0.000 description 1
108010067372 Pancreatic elastase Proteins 0.000 description 1
102000016387 Pancreatic elastase Human genes 0.000 description 1
108090000526 Papain Proteins 0.000 description 1
108090000284 Pepsin A Proteins 0.000 description 1
102000057297 Pepsin A Human genes 0.000 description 1
108010033276 Peptide Fragments Proteins 0.000 description 1
102000007079 Peptide Fragments Human genes 0.000 description 1
102000045595 Phosphoprotein Phosphatases Human genes 0.000 description 1
108700019535 Phosphoprotein Phosphatases Proteins 0.000 description 1
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 description 1
108700015930 Prolyl Oligopeptidases Proteins 0.000 description 1
102000056251 Prolyl Oligopeptidases Human genes 0.000 description 1
108010059712 Pronase Proteins 0.000 description 1
206010060862 Prostate cancer Diseases 0.000 description 1
208000000236 Prostatic Neoplasms Diseases 0.000 description 1
102000001253 Protein Kinase Human genes 0.000 description 1
240000004808 Saccharomyces cerevisiae Species 0.000 description 1
MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 1
108050000761 Serpin Proteins 0.000 description 1
102000008847 Serpin Human genes 0.000 description 1
101000895926 Streptomyces plicatus Endo-beta-N-acetylglucosaminidase H Proteins 0.000 description 1
108090001109 Thermolysin Proteins 0.000 description 1
108090000190 Thrombin Proteins 0.000 description 1
RHQDFWAXVIIEBN-UHFFFAOYSA-N Trifluoroethanol Chemical compound OCC(F)(F)F RHQDFWAXVIIEBN-UHFFFAOYSA-N 0.000 description 1
102100038968 WAP four-disulfide core domain protein 1 Human genes 0.000 description 1
230000037374 absorbed through the skin Effects 0.000 description 1
230000021736 acetylation Effects 0.000 description 1
238000006640 acetylation reaction Methods 0.000 description 1
230000009471 action Effects 0.000 description 1
230000006978 adaptation Effects 0.000 description 1
239000003463 adsorbent Substances 0.000 description 1
239000003513 alkali Substances 0.000 description 1
108091005588 alkylated proteins Proteins 0.000 description 1
AFVLVVWMAFSXCK-VMPITWQZSA-N alpha-cyano-4-hydroxycinnamic acid Chemical compound OC(=O)C(\C#N)=C\C1=CC=C(O)C=C1 AFVLVVWMAFSXCK-VMPITWQZSA-N 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
QGZKDVFQNNGYKY-UHFFFAOYSA-O ammonium group Chemical group [NH4+] QGZKDVFQNNGYKY-UHFFFAOYSA-O 0.000 description 1
210000004381 amniotic fluid Anatomy 0.000 description 1
150000001450 anions Chemical class 0.000 description 1
230000003466 anti-cipated effect Effects 0.000 description 1
229940124691 antibody therapeutics Drugs 0.000 description 1
102000036639 antigens Human genes 0.000 description 1
108091007433 antigens Proteins 0.000 description 1
238000013473 artificial intelligence Methods 0.000 description 1
235000009582 asparagine Nutrition 0.000 description 1
229960001230 asparagine Drugs 0.000 description 1
125000000613 asparagine group Chemical group N[C@@H](CC(N)=O)C(=O)* 0.000 description 1
SQVRNKJHWKZAKO-UHFFFAOYSA-N beta-N-Acetyl-D-neuraminic acid Natural products CC(=O)NC1C(O)CC(O)(C(O)=O)OC1C(O)C(O)CO SQVRNKJHWKZAKO-UHFFFAOYSA-N 0.000 description 1
108091008324 binding proteins Proteins 0.000 description 1
230000008827 biological function Effects 0.000 description 1
229960002685 biotin Drugs 0.000 description 1
235000020958 biotin Nutrition 0.000 description 1
239000011616 biotin Substances 0.000 description 1
230000000740 bleeding effect Effects 0.000 description 1
210000004369 blood Anatomy 0.000 description 1
239000008280 blood Substances 0.000 description 1
125000005621 boronate group Chemical group 0.000 description 1
239000006227 byproduct Substances 0.000 description 1
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 description 1
238000005341 cation exchange Methods 0.000 description 1
230000003915 cell function Effects 0.000 description 1
230000001413 cellular effect Effects 0.000 description 1
230000008859 change Effects 0.000 description 1
238000004182 chemical digestion Methods 0.000 description 1
238000001311 chemical methods and process Methods 0.000 description 1
HVYWMOMLDIMFJA-DPAQBDIFSA-N cholesterol group Chemical group [C@@H]1(CC[C@H]2[C@@H]3CC=C4C[C@@H](O)CC[C@]4(C)[C@H]3CC[C@]12C)[C@H](C)CCCC(C)C HVYWMOMLDIMFJA-DPAQBDIFSA-N 0.000 description 1
239000012501 chromatography medium Substances 0.000 description 1
229960002376 chymotrypsin Drugs 0.000 description 1
235000013985 cinnamic acid Nutrition 0.000 description 1
229930016911 cinnamic acid Natural products 0.000 description 1
229960002173 citrulline Drugs 0.000 description 1
235000013477 citrulline Nutrition 0.000 description 1
238000002288 cocrystallisation Methods 0.000 description 1
239000012468 concentrated sample Substances 0.000 description 1
230000002153 concerted effect Effects 0.000 description 1
239000000356 contaminant Substances 0.000 description 1
235000018417 cysteine Nutrition 0.000 description 1
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
238000013480 data collection Methods 0.000 description 1
230000006240 deamidation Effects 0.000 description 1
239000003398 denaturant Substances 0.000 description 1
239000013578 denaturing buffer Substances 0.000 description 1
238000000151 deposition Methods 0.000 description 1
238000011033 desalting Methods 0.000 description 1
238000013461 design Methods 0.000 description 1
229950006137 dexfosfoserine Drugs 0.000 description 1
238000003745 diagnosis Methods 0.000 description 1
125000003963 dichloro group Chemical group Cl* 0.000 description 1
SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
NLEBIOOXCVAHBD-QKMCSOCLSA-N dodecyl beta-D-maltoside Chemical compound O[C@@H]1[C@@H](O)[C@H](OCCCCCCCCCCCC)O[C@H](CO)[C@H]1O[C@@H]1[C@H](O)[C@@H](O)[C@H](O)[C@@H](CO)O1 NLEBIOOXCVAHBD-QKMCSOCLSA-N 0.000 description 1
239000003596 drug target Substances 0.000 description 1
238000001035 drying Methods 0.000 description 1
238000001962 electrophoresis Methods 0.000 description 1
210000002472 endoplasmic reticulum Anatomy 0.000 description 1
238000000605 extraction Methods 0.000 description 1
235000019253 formic acid Nutrition 0.000 description 1
238000013467 fragmentation Methods 0.000 description 1
238000006062 fragmentation reaction Methods 0.000 description 1
125000000524 functional group Chemical group 0.000 description 1
238000007429 general method Methods 0.000 description 1
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 1
RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 1
239000001963 growth medium Substances 0.000 description 1
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
238000004128 high performance liquid chromatography Methods 0.000 description 1
238000000265 homogenisation Methods 0.000 description 1
229940088597 hormone Drugs 0.000 description 1
239000005556 hormone Substances 0.000 description 1
231100000003 human carcinogen Toxicity 0.000 description 1
210000005260 human cell Anatomy 0.000 description 1
125000001165 hydrophobic group Chemical group 0.000 description 1
238000004191 hydrophobic interaction chromatography Methods 0.000 description 1
230000005661 hydrophobic surface Effects 0.000 description 1
125000002887 hydroxy group Chemical group [H]O* 0.000 description 1
210000000987 immune system Anatomy 0.000 description 1
238000003018 immunoassay Methods 0.000 description 1
230000006872 improvement Effects 0.000 description 1
239000012535 impurity Substances 0.000 description 1
230000005764 inhibitory process Effects 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
230000035992 intercellular communication Effects 0.000 description 1
230000003834 intracellular effect Effects 0.000 description 1
JDNTWHVOXJZDSN-UHFFFAOYSA-N iodoacetic acid Chemical compound OC(=O)CI JDNTWHVOXJZDSN-UHFFFAOYSA-N 0.000 description 1
235000014655 lactic acid Nutrition 0.000 description 1
239000004310 lactic acid Substances 0.000 description 1
238000004989 laser desorption mass spectroscopy Methods 0.000 description 1
150000007517 lewis acids Chemical class 0.000 description 1
150000007527 lewis bases Chemical class 0.000 description 1
150000002632 lipids Chemical class 0.000 description 1
238000004811 liquid chromatography Methods 0.000 description 1
238000004895 liquid chromatography mass spectrometry Methods 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
238000004519 manufacturing process Methods 0.000 description 1
238000005259 measurement Methods 0.000 description 1
239000002609 medium Substances 0.000 description 1
229960003151 mercaptamine Drugs 0.000 description 1
230000002503 metabolic effect Effects 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
229910021645 metal ion Inorganic materials 0.000 description 1
125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
WBYWAXJHAXSJNI-UHFFFAOYSA-N methyl p-hydroxycinnamate Natural products OC(=O)C=CC1=CC=CC=C1 WBYWAXJHAXSJNI-UHFFFAOYSA-N 0.000 description 1
238000005065 mining Methods 0.000 description 1
238000002156 mixing Methods 0.000 description 1
238000010369 molecular cloning Methods 0.000 description 1
230000001537 neural effect Effects 0.000 description 1
210000002445 nipple Anatomy 0.000 description 1
238000002414 normal-phase solid-phase extraction Methods 0.000 description 1
229960003104 ornithine Drugs 0.000 description 1
IFPHDUVGLXEIOQ-UHFFFAOYSA-N ortho-iodosylbenzoic acid Chemical compound OC(=O)C1=CC=CC=C1I=O IFPHDUVGLXEIOQ-UHFFFAOYSA-N 0.000 description 1
230000002611 ovarian Effects 0.000 description 1
230000003647 oxidation Effects 0.000 description 1
238000007254 oxidation reaction Methods 0.000 description 1
229940055729 papain Drugs 0.000 description 1
235000019834 papain Nutrition 0.000 description 1
229940111202 pepsin Drugs 0.000 description 1
239000004033 plastic Substances 0.000 description 1
229920003023 plastic Polymers 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
239000000256 polyoxyethylene sorbitan monolaurate Substances 0.000 description 1
102000035123 post-translationally modified proteins Human genes 0.000 description 1
108091005626 post-translationally modified proteins Proteins 0.000 description 1
ZNNZYHKDIALBAK-UHFFFAOYSA-M potassium thiocyanate Chemical compound [K+].[S-]C#N ZNNZYHKDIALBAK-UHFFFAOYSA-M 0.000 description 1
229940116357 potassium thiocyanate Drugs 0.000 description 1
230000013823 prenylation Effects 0.000 description 1
238000012545 processing Methods 0.000 description 1
210000002307 prostate Anatomy 0.000 description 1
235000019419 proteases Nutrition 0.000 description 1
125000006239 protecting group Chemical group 0.000 description 1
238000003498 protein array Methods 0.000 description 1
238000012514 protein characterization Methods 0.000 description 1
238000000751 protein extraction Methods 0.000 description 1
230000007065 protein hydrolysis Effects 0.000 description 1
108060006633 protein kinase Proteins 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
239000012460 protein solution Substances 0.000 description 1
238000001243 protein synthesis Methods 0.000 description 1
229950010131 puromycin Drugs 0.000 description 1
GRJJQCWNZGRKAU-UHFFFAOYSA-N pyridin-1-ium;fluoride Chemical compound F.C1=CC=NC=C1 GRJJQCWNZGRKAU-UHFFFAOYSA-N 0.000 description 1
UMJSCPRVCHMLSP-UHFFFAOYSA-N pyridine Natural products COC1=CC=CN=C1 UMJSCPRVCHMLSP-UHFFFAOYSA-N 0.000 description 1
238000003908 quality control method Methods 0.000 description 1
239000000376 reactant Substances 0.000 description 1
239000005871 repellent Substances 0.000 description 1
239000004576 sand Substances 0.000 description 1
238000012216 screening Methods 0.000 description 1
229940055619 selenocysteine Drugs 0.000 description 1
235000016491 selenocysteine Nutrition 0.000 description 1
ZKZBPNGNEQAJSX-UHFFFAOYSA-N selenocysteine Natural products [SeH]CC(N)C(O)=O ZKZBPNGNEQAJSX-UHFFFAOYSA-N 0.000 description 1
210000000582 semen Anatomy 0.000 description 1
238000011896 sensitive detection Methods 0.000 description 1
239000003001 serine protease inhibitor Substances 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
125000005629 sialic acid group Chemical group 0.000 description 1
125000005630 sialyl group Chemical group 0.000 description 1
238000007086 side reaction Methods 0.000 description 1
230000011664 signaling Effects 0.000 description 1
150000003384 small molecules Chemical class 0.000 description 1
235000009518 sodium iodide Nutrition 0.000 description 1
239000007790 solid phase Substances 0.000 description 1
238000005063 solubilization Methods 0.000 description 1
230000007928 solubilization Effects 0.000 description 1
230000003381 solubilizing effect Effects 0.000 description 1
239000002904 solvent Substances 0.000 description 1
241000894007 species Species 0.000 description 1
238000004611 spectroscopical analysis Methods 0.000 description 1
238000010183 spectrum analysis Methods 0.000 description 1
238000013222 sprague-dawley male rat Methods 0.000 description 1
238000012453 sprague-dawley rat model Methods 0.000 description 1
239000007921 spray Substances 0.000 description 1
230000007480 spreading Effects 0.000 description 1
238000003892 spreading Methods 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
238000010561 standard procedure Methods 0.000 description 1
DFVFTMTWCUHJBL-BQBZGAKWSA-N statine Chemical compound CC(C)C[C@H](N)[C@@H](O)CC(O)=O DFVFTMTWCUHJBL-BQBZGAKWSA-N 0.000 description 1
FRGKKTITADJNOE-UHFFFAOYSA-N sulfanyloxyethane Chemical compound CCOS FRGKKTITADJNOE-UHFFFAOYSA-N 0.000 description 1
125000001273 sulfonato group Chemical group [O-]S(*)(=O)=O 0.000 description 1
230000010741 sumoylation Effects 0.000 description 1
210000001179 synovial fluid Anatomy 0.000 description 1
125000000101 thioether group Chemical group 0.000 description 1
125000003396 thiol group Chemical group [H]S* 0.000 description 1
150000003573 thiols Chemical class 0.000 description 1
229960004072 thrombin Drugs 0.000 description 1
231100000167 toxic agent Toxicity 0.000 description 1
239000003440 toxic substance Substances 0.000 description 1
231100000419 toxicity Toxicity 0.000 description 1
230000001988 toxicity Effects 0.000 description 1
230000014616 translation Effects 0.000 description 1
TUQOTMZNTHZOKS-UHFFFAOYSA-N tributylphosphine Chemical compound CCCCP(CCCC)CCCC TUQOTMZNTHZOKS-UHFFFAOYSA-N 0.000 description 1
YNJBWRMUSHSURL-UHFFFAOYSA-N trichloroacetic acid Chemical class OC(=O)C(Cl)(Cl)Cl YNJBWRMUSHSURL-UHFFFAOYSA-N 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
239000000107 tumor biomarker Substances 0.000 description 1
238000000539 two dimensional gel electrophoresis Methods 0.000 description 1
125000001493 tyrosinyl group Chemical group [H]OC1=C([H])C([H])=C(C([H])=C1[H])C([H])([H])C([H])(N([H])[H])C(*)=O 0.000 description 1
230000034512 ubiquitination Effects 0.000 description 1
238000010798 ubiquitination Methods 0.000 description 1
239000012808 vapor phase Substances 0.000 description 1

Classifications

- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6842—Proteomic analysis of subsets of protein mixtures with reduced complexity, e.g. membrane proteins, phosphoproteins, organelle proteins
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N33/00—Investigating or analysing materials by specific methods not covered by groups G01N1/00 - G01N31/00
- G01N33/48—Biological material, e.g. blood, urine; Haemocytometers
- G01N33/50—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing
- G01N33/68—Chemical analysis of biological material, e.g. blood, urine; Testing involving biospecific ligand binding methods; Immunological testing involving proteins, peptides or amino acids
- G01N33/6803—General methods of protein analysis not limited to specific proteins or families of proteins
- G01N33/6848—Methods of protein analysis involving mass spectrometry

Landscapes

Life Sciences & Earth Sciences (AREA)
Health & Medical Sciences (AREA)
Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Physics & Mathematics (AREA)
Hematology (AREA)
Chemical & Material Sciences (AREA)
Biomedical Technology (AREA)
Urology & Nephrology (AREA)
Immunology (AREA)
Bioinformatics & Cheminformatics (AREA)
Bioinformatics & Computational Biology (AREA)
Biophysics (AREA)
Analytical Chemistry (AREA)
Pathology (AREA)
Biotechnology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Food Science & Technology (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
Microbiology (AREA)
General Physics & Mathematics (AREA)
Cell Biology (AREA)
Spectroscopy & Molecular Physics (AREA)
Investigating Or Analysing Biological Materials (AREA)
Other Investigation Or Analysis Of Materials By Electrical Means (AREA)

CA 2507117 2005-05-11 2005-05-11 Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines Abandoned CA2507117A1 (fr)

Priority Applications (2)

Application Number	Priority Date	Filing Date	Title
CA 2507117 CA2507117A1 (fr)	2005-05-11	2005-05-11	Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines
US11/431,820 US7622273B2 (en)	2005-05-11	2006-05-11	Method for chemical and enzymatic treatment of posttranslationally modified proteins bound to a protein chip

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
CA 2507117 CA2507117A1 (fr)	2005-05-11	2005-05-11	Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines

Publications (1)

Publication Number	Publication Date
CA2507117A1 true CA2507117A1 (fr)	2006-11-11

Family

ID=37441446

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
CA 2507117 Abandoned CA2507117A1 (fr)	2005-05-11	2005-05-11	Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines

Country Status (1)

Country	Link
CA (1)	CA2507117A1 (fr)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN103852527A (zh) *	2012-12-05	2014-06-11	中国科学院大连化学物理研究所	一种高通量蛋白质样品预处理装置
WO2018090651A1 (fr) *	2016-11-21	2018-05-24	中国科学院大连化学物理研究所	Procédé de prétraitement de protéine dans un liquide organique ex vivo

2005
- 2005-05-11 CA CA 2507117 patent/CA2507117A1/fr not_active Abandoned

Cited By (4)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
CN103852527A (zh) *	2012-12-05	2014-06-11	中国科学院大连化学物理研究所	一种高通量蛋白质样品预处理装置
CN103852527B (zh) *	2012-12-05	2015-05-13	中国科学院大连化学物理研究所	一种高通量蛋白质样品预处理装置
WO2018090651A1 (fr) *	2016-11-21	2018-05-24	中国科学院大连化学物理研究所	Procédé de prétraitement de protéine dans un liquide organique ex vivo
US11365214B2 (en)	2016-11-21	2022-06-21	Dalian Institute Of Chemical Physics, Chinese Academy Of Sciences	Method for pretreating protein in ex vivo body fluid

Legal Events

Date	Code	Title	Description
2007-05-11	EEER	Examination request
2012-09-14	FZDE	Dead

Publication	Publication Date	Title
US7622273B2 (en)	2009-11-24	Method for chemical and enzymatic treatment of posttranslationally modified proteins bound to a protein chip
US7183118B2 (en)	2007-02-27	Methods for quantitative proteome analysis of glycoproteins
Dalpathado et al.	2008	Glycopeptide analysis by mass spectrometry
Palmisano et al.	2013	Structural analysis of glycoprotein sialylation–part II: LC-MS based detection
Fenselau	1997	Peer reviewed: MALDI MS and strategies for protein analysis
Ashcroft	2003	Protein and peptide identification: the role of mass spectrometry in proteomics
US20070269895A1 (en)	2007-11-22	Methods for quantitative proteome analysis of glycoproteins
Lee et al.	2005	Immobilization of aminophenylboronic acid on magnetic beads for the direct determination of glycoproteins by matrix assisted laser desorption ionization mass spectrometry
Gooley et al.	1997	The importance of protein co-and post-translational modifications in proteome projects
EP2087357A1 (fr)	2009-08-12	Composés et procédés de double marquage de polypeptides pour permettre le multiplexage en analyse spectrométrique de masse
EP3519832B1 (fr)	2024-04-03	Complexes de glycane et d'acides aminés marqués utiles dans l'analyse en lc-sm et procédés pour les préparer
US20050095661A1 (en)	2005-05-05	Method for characterizing polypeptides
JP2004505248A (ja)	2004-02-19	ポリペプチドの配列決定のための新しい方法及びキット
Salzano et al.	2005	Mass spectrometry for protein identification and the study of post translational modifications
WO2002059144A2 (fr)	2002-08-01	Marquage differentiel pour l'analyse de melanges proteiniques complexes
US8097463B2 (en)	2012-01-17	Use of arylboronic acids in protein labelling
CA2507117A1 (fr)	2006-11-11	Traitement chimique et enzymatique complet de proteines glycolysees et phosphorylees sur des biopuces de proteines
Kussmann et al.	1998	Characterisation of the covalent structure of proteins from biological material by MALDI mass spectrometry‣ possibilities and limitations
EP1525483A2 (fr)	2005-04-27	Etiquetage differentiel pour l'analyse quantitative de melanges complexes de proteinesen utilisant comme reactif des peptides synthetiques comprenant des groupes iodoacetamido
EP1748297B1 (fr)	2010-06-23	Procédé d'analyse des peptides d'origine naturelle et petits peptides par spectrométrie de masse
Ge et al.	2005	Complete chemical and enzymatic treatment of phosphorylated and glycosylated proteins on proteinchip arrays
Armirotti	2009	Bottom-up proteomics
US20060024660A1 (en)	2006-02-02	Method for relative quantification of proteins
Steckel et al.	2020	Detection of protein posttranslational modifications by mass spectrometry
Leijten	2021	Diving into cellular signalling: Functional proteome analysis by mass spectrometry based approaches