NO322326B1 - Fremgangsmate for rensing av korrekt foldet monomer - insulinlignende vekstfaktor-1 (IGF-1) - Google Patents

Fremgangsmate for rensing av korrekt foldet monomer - insulinlignende vekstfaktor-1 (IGF-1) Download PDF

Info

Publication number: NO322326B1
Authority: NO; Norway
Prior art keywords: igf; matrix; cation exchange; authentic; buffer
Prior art date: 1995-04-14

Application number

NO19974740A

Other languages

English (en)

Norwegian (no)

Other versions

NO974740D0 (no

NO974740L (no

Inventor

Cynthia Ann Cowgill

Glenn Dorin

Russell A Brierley

Joan N Abrams

John M Hanson

Francis C Maslanka

Luis Juarbe-Osorio

Patricio Riquelme

Original Assignee

Cephalon Inc

Chiron Corp

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.)

1995-04-14

Filing date

1997-10-13

Publication date

2006-09-18

1997-10-13 Application filed by Cephalon Inc, Chiron Corp filed Critical Cephalon Inc

1997-10-13 Publication of NO974740D0 publication Critical patent/NO974740D0/no

1997-12-12 Publication of NO974740L publication Critical patent/NO974740L/no

2006-09-18 Publication of NO322326B1 publication Critical patent/NO322326B1/no

Links

238000000034 method Methods 0.000 title claims abstract description 113
101000599951 Homo sapiens Insulin-like growth factor I Proteins 0.000 title claims description 14
102100037852 Insulin-like growth factor I Human genes 0.000 title claims description 8
238000000746 purification Methods 0.000 title description 10
239000000178 monomer Substances 0.000 title description 6
102000004218 Insulin-Like Growth Factor I Human genes 0.000 claims abstract description 258
108090000723 Insulin-Like Growth Factor I Proteins 0.000 claims abstract description 258
238000005341 cation exchange Methods 0.000 claims abstract description 89
238000004191 hydrophobic interaction chromatography Methods 0.000 claims abstract description 54
238000004366 reverse phase liquid chromatography Methods 0.000 claims abstract description 27
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 claims description 92
239000011159 matrix material Substances 0.000 claims description 87
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 77
235000002639 sodium chloride Nutrition 0.000 claims description 57
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical group CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 claims description 51
239000011780 sodium chloride Substances 0.000 claims description 39
239000000463 material Substances 0.000 claims description 38
239000000872 buffer Substances 0.000 claims description 29
238000005406 washing Methods 0.000 claims description 28
239000012504 chromatography matrix Substances 0.000 claims description 25
239000002609 medium Substances 0.000 claims description 24
239000012149 elution buffer Substances 0.000 claims description 18
150000003839 salts Chemical class 0.000 claims description 18
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 claims description 15
KFZMGEQAYNKOFK-UHFFFAOYSA-N Isopropanol Chemical compound CC(C)O KFZMGEQAYNKOFK-UHFFFAOYSA-N 0.000 claims description 12
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 claims description 12
VMHLLURERBWHNL-UHFFFAOYSA-M Sodium acetate Chemical compound [Na+].CC([O-])=O VMHLLURERBWHNL-UHFFFAOYSA-M 0.000 claims description 12
239000001632 sodium acetate Substances 0.000 claims description 12
235000017281 sodium acetate Nutrition 0.000 claims description 12
238000010828 elution Methods 0.000 claims description 11
239000011534 wash buffer Substances 0.000 claims description 11
230000002209 hydrophobic effect Effects 0.000 claims description 10
210000005253 yeast cell Anatomy 0.000 claims description 9
239000002253 acid Substances 0.000 claims description 8
238000010405 reoxidation reaction Methods 0.000 claims description 8
238000001179 sorption measurement Methods 0.000 claims description 8
230000003993 interaction Effects 0.000 claims description 7
239000003960 organic solvent Substances 0.000 claims description 7
239000007974 sodium acetate buffer Substances 0.000 claims description 7
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims description 6
239000004202 carbamide Substances 0.000 claims description 6
241000235058 Komagataella pastoris Species 0.000 claims description 5
229910021538 borax Inorganic materials 0.000 claims description 5
235000010339 sodium tetraborate Nutrition 0.000 claims description 5
239000002904 solvent Substances 0.000 claims description 5
BSVBQGMMJUBVOD-UHFFFAOYSA-N trisodium borate Chemical compound [Na+].[Na+].[Na+].[O-]B([O-])[O-] BSVBQGMMJUBVOD-UHFFFAOYSA-N 0.000 claims description 5
238000004587 chromatography analysis Methods 0.000 claims description 4
239000001963 growth medium Substances 0.000 claims description 4
QTBSBXVTEAMEQO-UHFFFAOYSA-M Acetate Chemical compound CC([O-])=O QTBSBXVTEAMEQO-UHFFFAOYSA-M 0.000 claims description 3
240000004808 Saccharomyces cerevisiae Species 0.000 claims description 3
238000004925 denaturation Methods 0.000 claims description 3
230000036425 denaturation Effects 0.000 claims description 3
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 claims description 3
239000002952 polymeric resin Substances 0.000 claims description 3
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239000012062 aqueous buffer Substances 0.000 claims description 2
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238000005277 cation exchange chromatography Methods 0.000 abstract description 5
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238000006467 substitution reaction Methods 0.000 abstract 1
239000000047 product Substances 0.000 description 27
125000004093 cyano group Chemical group *C#N 0.000 description 22
238000004458 analytical method Methods 0.000 description 12
239000000243 solution Substances 0.000 description 12
238000000855 fermentation Methods 0.000 description 11
230000004151 fermentation Effects 0.000 description 11
210000004027 cell Anatomy 0.000 description 9
238000012510 peptide mapping method Methods 0.000 description 9
235000018102 proteins Nutrition 0.000 description 9
102000004169 proteins and genes Human genes 0.000 description 9
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238000004007 reversed phase HPLC Methods 0.000 description 7
238000012360 testing method Methods 0.000 description 7
238000002523 gelfiltration Methods 0.000 description 6
102000044162 human IGF1 Human genes 0.000 description 6
108010076504 Protein Sorting Signals Proteins 0.000 description 5
238000011026 diafiltration Methods 0.000 description 5
239000012528 membrane Substances 0.000 description 5
229920000936 Agarose Polymers 0.000 description 4
238000002965 ELISA Methods 0.000 description 4
XEEYBQQBJWHFJM-UHFFFAOYSA-N Iron Chemical compound [Fe] XEEYBQQBJWHFJM-UHFFFAOYSA-N 0.000 description 4
QAOWNCQODCNURD-UHFFFAOYSA-N Sulfuric acid Chemical compound OS(O)(=O)=O QAOWNCQODCNURD-UHFFFAOYSA-N 0.000 description 4
230000004888 barrier function Effects 0.000 description 4
-1 butyl- Chemical group 0.000 description 4
239000012467 final product Substances 0.000 description 4
238000004128 high performance liquid chromatography Methods 0.000 description 4
108090000765 processed proteins & peptides Proteins 0.000 description 4
239000000523 sample Substances 0.000 description 4
101150051118 PTM1 gene Proteins 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 3
BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 3
229910052921 ammonium sulfate Inorganic materials 0.000 description 3
235000011130 ammonium sulphate Nutrition 0.000 description 3
125000000484 butyl group Chemical group [H]C([*])([H])C([H])([H])C([H])([H])C([H])([H])[H] 0.000 description 3
239000000356 contaminant Substances 0.000 description 3
125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 3
239000013604 expression vector Substances 0.000 description 3
238000010829 isocratic elution Methods 0.000 description 3
238000001155 isoelectric focusing Methods 0.000 description 3
238000011068 loading method Methods 0.000 description 3
238000004519 manufacturing process Methods 0.000 description 3
238000011084 recovery Methods 0.000 description 3
230000009467 reduction Effects 0.000 description 3
238000003998 size exclusion chromatography high performance liquid chromatography Methods 0.000 description 3
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 3
239000007858 starting material Substances 0.000 description 3
101100322245 Caenorhabditis elegans des-2 gene Proteins 0.000 description 2
RYGMFSIKBFXOCR-UHFFFAOYSA-N Copper Chemical compound [Cu] RYGMFSIKBFXOCR-UHFFFAOYSA-N 0.000 description 2
229920002307 Dextran Polymers 0.000 description 2
ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 2
239000004793 Polystyrene Substances 0.000 description 2
PMZURENOXWZQFD-UHFFFAOYSA-L Sodium Sulfate Chemical compound [Na+].[Na+].[O-]S([O-])(=O)=O PMZURENOXWZQFD-UHFFFAOYSA-L 0.000 description 2
HCHKCACWOHOZIP-UHFFFAOYSA-N Zinc Chemical compound [Zn] HCHKCACWOHOZIP-UHFFFAOYSA-N 0.000 description 2
125000003275 alpha amino acid group Chemical group 0.000 description 2
125000000539 amino acid group Chemical group 0.000 description 2
239000006172 buffering agent Substances 0.000 description 2
239000001913 cellulose Substances 0.000 description 2
229920002678 cellulose Polymers 0.000 description 2
238000005119 centrifugation Methods 0.000 description 2
238000012512 characterization method Methods 0.000 description 2
239000003795 chemical substances by application Substances 0.000 description 2
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238000004140 cleaning Methods 0.000 description 2
229910052802 copper Inorganic materials 0.000 description 2
239000010949 copper Substances 0.000 description 2
238000011161 development Methods 0.000 description 2
230000018109 developmental process Effects 0.000 description 2
239000013542 high molecular weight contaminant Substances 0.000 description 2
239000012510 hollow fiber Substances 0.000 description 2
239000012535 impurity Substances 0.000 description 2
229910052742 iron Inorganic materials 0.000 description 2
230000014759 maintenance of location Effects 0.000 description 2
238000004949 mass spectrometry Methods 0.000 description 2
230000002297 mitogenic effect Effects 0.000 description 2
239000000203 mixture Substances 0.000 description 2
239000008363 phosphate buffer Substances 0.000 description 2
229920002492 poly(sulfone) Polymers 0.000 description 2
229920001184 polypeptide Polymers 0.000 description 2
229920002223 polystyrene Polymers 0.000 description 2
239000002243 precursor Substances 0.000 description 2
102000004196 processed proteins & peptides Human genes 0.000 description 2
230000008929 regeneration Effects 0.000 description 2
238000011069 regeneration method Methods 0.000 description 2
239000012488 sample solution Substances 0.000 description 2
230000028327 secretion Effects 0.000 description 2
238000012163 sequencing technique Methods 0.000 description 2
229910052938 sodium sulfate Inorganic materials 0.000 description 2
235000011152 sodium sulphate Nutrition 0.000 description 2
239000000126 substance Substances 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
238000000108 ultra-filtration Methods 0.000 description 2
238000001262 western blot Methods 0.000 description 2
239000011701 zinc Substances 0.000 description 2
229910052725 zinc Inorganic materials 0.000 description 2
SKLHQIMWCOGGKH-UHFFFAOYSA-O 2-[2,3-dimethyl-6-(5-phenyl-2H-tetrazol-1-ium-1-yl)phenyl]-1,3-thiazole Chemical compound CC1=C(C(=C(C=C1)[N+]=1NN=NC=1C1=CC=CC=C1)C=1SC=CN=1)C SKLHQIMWCOGGKH-UHFFFAOYSA-O 0.000 description 1
USFZMSVCRYTOJT-UHFFFAOYSA-N Ammonium acetate Chemical compound N.CC(O)=O USFZMSVCRYTOJT-UHFFFAOYSA-N 0.000 description 1
239000005695 Ammonium acetate Substances 0.000 description 1
BTBUEUYNUDRHOZ-UHFFFAOYSA-N Borate Chemical compound [O-]B([O-])[O-] BTBUEUYNUDRHOZ-UHFFFAOYSA-N 0.000 description 1
VYZAMTAEIAYCRO-UHFFFAOYSA-N Chromium Chemical compound [Cr] VYZAMTAEIAYCRO-UHFFFAOYSA-N 0.000 description 1
230000010777 Disulfide Reduction Effects 0.000 description 1
241000588724 Escherichia coli Species 0.000 description 1
101150088952 IGF1 gene Proteins 0.000 description 1
CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
125000001429 N-terminal alpha-amino-acid group Chemical group 0.000 description 1
241000235648 Pichia Species 0.000 description 1
239000007983 Tris buffer Substances 0.000 description 1
239000008351 acetate buffer Substances 0.000 description 1
150000007513 acids Chemical class 0.000 description 1
230000004913 activation Effects 0.000 description 1
229910000147 aluminium phosphate Inorganic materials 0.000 description 1
235000019257 ammonium acetate Nutrition 0.000 description 1
229940043376 ammonium acetate Drugs 0.000 description 1
238000004166 bioassay Methods 0.000 description 1
230000004071 biological effect Effects 0.000 description 1
230000015572 biosynthetic process Effects 0.000 description 1
238000004364 calculation method Methods 0.000 description 1
125000000837 carbohydrate group Chemical group 0.000 description 1
210000000170 cell membrane Anatomy 0.000 description 1
230000003196 chaotropic effect Effects 0.000 description 1
239000003638 chemical reducing agent Substances 0.000 description 1
210000002932 cholinergic neuron Anatomy 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
239000012141 concentrate 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
238000010908 decantation Methods 0.000 description 1
238000011082 depyrogenation Methods 0.000 description 1
238000000502 dialysis Methods 0.000 description 1
238000010790 dilution Methods 0.000 description 1
239000012895 dilution Substances 0.000 description 1
SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 description 1
230000003292 diminished effect Effects 0.000 description 1
239000003480 eluent Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
210000003527 eukaryotic cell Anatomy 0.000 description 1
238000002474 experimental method Methods 0.000 description 1
210000003722 extracellular fluid Anatomy 0.000 description 1
238000001914 filtration Methods 0.000 description 1
230000004907 flux Effects 0.000 description 1
238000009472 formulation Methods 0.000 description 1
239000012634 fragment Substances 0.000 description 1
239000000499 gel Substances 0.000 description 1
239000003102 growth factor Substances 0.000 description 1
238000010348 incorporation Methods 0.000 description 1
230000002608 insulinlike Effects 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
238000013507 mapping Methods 0.000 description 1
238000001471 micro-filtration Methods 0.000 description 1
239000003226 mitogen Substances 0.000 description 1
238000002156 mixing Methods 0.000 description 1
210000003205 muscle Anatomy 0.000 description 1
239000013642 negative control Substances 0.000 description 1
210000002569 neuron Anatomy 0.000 description 1
230000000263 nonmitogenic effect Effects 0.000 description 1
238000005457 optimization Methods 0.000 description 1
201000008968 osteosarcoma Diseases 0.000 description 1
239000013612 plasmid Substances 0.000 description 1
239000011148 porous material Substances 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
OTYBMLCTZGSZBG-UHFFFAOYSA-L potassium sulfate Chemical compound [K+].[K+].[O-]S([O-])(=O)=O OTYBMLCTZGSZBG-UHFFFAOYSA-L 0.000 description 1
229910052939 potassium sulfate Inorganic materials 0.000 description 1
235000011151 potassium sulphates Nutrition 0.000 description 1
230000003389 potentiating effect Effects 0.000 description 1
238000001556 precipitation Methods 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
238000001742 protein purification Methods 0.000 description 1
230000030788 protein refolding Effects 0.000 description 1
238000000734 protein sequencing Methods 0.000 description 1
230000006432 protein unfolding Effects 0.000 description 1
230000007017 scission Effects 0.000 description 1
150000003384 small molecules Chemical class 0.000 description 1
239000001509 sodium citrate Substances 0.000 description 1
NLJMYIDDQXHKNR-UHFFFAOYSA-K sodium citrate Chemical compound O.O.[Na+].[Na+].[Na+].[O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O NLJMYIDDQXHKNR-UHFFFAOYSA-K 0.000 description 1
235000011083 sodium citrates Nutrition 0.000 description 1
230000003381 solubilizing effect Effects 0.000 description 1
238000003756 stirring Methods 0.000 description 1
230000004083 survival effect Effects 0.000 description 1
229920001059 synthetic polymer Polymers 0.000 description 1
210000001519 tissue Anatomy 0.000 description 1
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
238000000870 ultraviolet spectroscopy Methods 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/575—Hormones
- C07K14/65—Insulin-like growth factors, i.e. somatomedins, e.g. IGF-1, IGF-2
- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N30/00—Investigating or analysing materials by separation into components using adsorption, absorption or similar phenomena or using ion-exchange, e.g. chromatography or field flow fractionation
- G01N30/02—Column chromatography

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Zoology (AREA)
Molecular Biology (AREA)
Gastroenterology & Hepatology (AREA)
Endocrinology (AREA)
Biochemistry (AREA)
Biophysics (AREA)
General Health & Medical Sciences (AREA)
Genetics & Genomics (AREA)
Medicinal Chemistry (AREA)
Toxicology (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Diabetes (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Nitrogen And Oxygen Or Sulfur-Condensed Heterocyclic Ring Systems (AREA)
Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Nitrogen Condensed Heterocyclic Rings (AREA)

NO19974740A 1995-04-14 1997-10-13 Fremgangsmate for rensing av korrekt foldet monomer - insulinlignende vekstfaktor-1 (IGF-1) NO322326B1 (no)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US08/422,436 US5650496A (en)	1995-04-14	1995-04-14	IGF-I purification process
PCT/US1996/005099 WO1996032407A1 (en)	1995-04-14	1996-04-12	Igf-i purification process

Publications (3)

Publication Number	Publication Date
NO974740D0 NO974740D0 (no)	1997-10-13
NO974740L NO974740L (no)	1997-12-12
NO322326B1 true NO322326B1 (no)	2006-09-18

Family

ID=23674879

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
NO19974740A NO322326B1 (no)	1995-04-14	1997-10-13	Fremgangsmate for rensing av korrekt foldet monomer - insulinlignende vekstfaktor-1 (IGF-1)

Country Status (11)

Country	Link
US (2)	US5650496A (de)
EP (1)	EP0820463B1 (de)
JP (1)	JP3894570B2 (de)
AT (1)	ATE415411T1 (de)
AU (2)	AU696516B2 (de)
CA (1)	CA2218111C (de)
DE (1)	DE69637760D1 (de)
ES (1)	ES2321242T3 (de)
NO (1)	NO322326B1 (de)
NZ (1)	NZ306782A (de)
WO (1)	WO1996032407A1 (de)

Families Citing this family (23)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
WO1996007744A1 (en) *	1994-09-08	1996-03-14	Chiron Corporation	A method of improved production of insulin-like growth factor
US6756484B1 (en)	1995-04-14	2004-06-29	Cephalon, Inc.	IGF-I purification process
US7071313B1 (en) *	1995-06-07	2006-07-04	Cephalon, Inc.	Methods of purifying authentic IGF from yeast hosts
US7193042B1 (en)	1995-06-07	2007-03-20	Chiron Corporation	Methods for purifying authentic IGF from yeast hosts
WO1996040776A1 (en) *	1995-06-07	1996-12-19	Chiron Corporation	Methods for purifying authentic igf from yeast hosts
AU729459B2 (en) *	1996-11-15	2001-02-01	Genentech Inc.	Purification of neurotrophins
JP2003530316A (ja)	1999-12-22	2003-10-14	ノボノルディスクアクティーゼルスカブ	スクランブルした一本鎖ポリペプチドの抽出的再生法
GB0011278D0 (en)	2000-05-10	2000-06-28	Univ London	Repair of nerve damage
WO2002009738A1 (en)	2000-07-28	2002-02-07	Murphy Christopher J	Transplant media
US20040203115A1 (en) *	2001-10-09	2004-10-14	Giardina Steven L	Methods and compositions for production and purification of recombinant staphylococcal enterotoxin b (rseb)
KR20030044696A (ko) *	2001-11-30	2003-06-09	정종문	피키아 파스토리스에서 재조합 인슐린 유사 성장인자-1단백질을 연속적으로 생산하는 방법
GB0202906D0 (en) *	2002-02-07	2002-03-27	Univ London	Prevention of myocardial damage
US7229554B2 (en) *	2002-09-25	2007-06-12	Novo Nordisk A/S	Purification process comprising microfiltration at elevated temperatures
US20070207209A1 (en) *	2004-08-27	2007-09-06	Murphy Christopher J	Trophic factor combinations for nervous system treatment
WO2006097682A1 (en) *	2005-03-18	2006-09-21	Ucl Business Plc	Mechano growth factor peptides and their use
KR102178191B1 (ko)	2008-09-02	2020-11-13	머크 밀리포어 리미티드	크로마토그래피 막, 이를 포함하는 장치 및 이의 이용방법
ES2543457T5 (es) *	2009-02-19	2021-12-22	Xellia Pharmaceuticals Aps	Procedimiento para purificar lipopéptidos
CA2780095C (en) *	2009-11-13	2018-12-11	Merck Millipore Ltd.	Hydrophobic interaction chromatography membranes, and methods of use thereof
US9873088B2 (en)	2011-05-17	2018-01-23	Natrix Separations Inc.	Layered tubular membranes for chromatography, and methods of use thereof
CA3233933A1 (en) *	2017-01-30	2018-08-02	Regeneron Pharmaceuticals, Inc.	Compositions and methods for reducing bioburden in chromatography
JP2020099909A (ja) *	2020-03-17	2020-07-02	ＨＯＹＡＴｅｃｈｎｏｓｕｒｇｉｃａｌ株式会社	処理方法、生産方法およびハイドロキシアパタイト充填剤
KR102933055B1 (ko) *	2020-11-05	2026-02-27	시믹 홀딩스 씨오., 엘티디.	재조합 인슐린 유사 성장 인자 i의 제조 방법
CN116754678B (zh) *	2023-06-19	2025-09-16	杭州度安医学检验实验室有限公司	一种血液中胰岛素样生长因子检测样本的处理及检测方法

Family Cites Families (10)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5093317A (en) *	1989-06-05	1992-03-03	Cephalon, Inc.	Treating disorders by application of insulin-like growth factor
WO1992003477A1 (en) *	1990-08-20	1992-03-05	Novo Nordisk A/S	Biologically active compound, a process for the preparation thereof and use of the same
CA2090969C (en) *	1990-09-04	2001-08-21	Russell Arthur Brierley	Production of insulin-like growth factor-1 in methylotrophic yeast cells
US5231178A (en) *	1991-01-16	1993-07-27	The Salk Institute Biotechnology/Industrial Associates, Inc.	Method for the purification of intact, correctly-folded insulin-like growth factor-1
US5288931A (en) *	1991-12-06	1994-02-22	Genentech, Inc.	Method for refolding insoluble, misfolded insulin-like growth factor-I into an active conformation
AU3812993A (en) *	1992-03-24	1993-10-21	Synergen, Inc.	Refolding and purification of insulin-like growth factor I
US5407810A (en) *	1993-08-20	1995-04-18	Genentech, Inc.	Aqueous multiple-phase isolation of polypeptide
US5663304A (en) *	1993-08-20	1997-09-02	Genentech, Inc.	Refolding of misfolded insulin-like growth factor-I
US5451660A (en) *	1993-12-13	1995-09-19	Genentech, Inc.	Method for purifying polypeptides
US5446024A (en) *	1993-12-17	1995-08-29	Genentech, Inc.	Purification of insulin-like growth factor

1995
- 1995-04-14 US US08/422,436 patent/US5650496A/en not_active Expired - Lifetime
1996
- 1996-04-12 WO PCT/US1996/005099 patent/WO1996032407A1/en not_active Ceased
- 1996-04-12 ES ES96912727T patent/ES2321242T3/es not_active Expired - Lifetime
- 1996-04-12 NZ NZ306782A patent/NZ306782A/en not_active IP Right Cessation
- 1996-04-12 CA CA002218111A patent/CA2218111C/en not_active Expired - Lifetime
- 1996-04-12 JP JP53122996A patent/JP3894570B2/ja not_active Expired - Lifetime
- 1996-04-12 DE DE69637760T patent/DE69637760D1/de not_active Expired - Lifetime
- 1996-04-12 AU AU55433/96A patent/AU696516B2/en not_active Revoked
- 1996-04-12 EP EP96912727A patent/EP0820463B1/de not_active Expired - Lifetime
- 1996-04-12 AT AT96912727T patent/ATE415411T1/de not_active IP Right Cessation
1997
- 1997-05-05 US US08/851,162 patent/US6207806B1/en not_active Expired - Lifetime
- 1997-10-13 NO NO19974740A patent/NO322326B1/no not_active IP Right Cessation
2007
- 2007-03-23 AU AU2007201259A patent/AU2007201259A1/en active Pending

Also Published As

Publication number	Publication date
EP0820463A4 (de)	2001-08-08
CA2218111C (en)	2008-07-08
AU2007201259A1 (en)	2007-04-05
EP0820463B1 (de)	2008-11-26
EP0820463A1 (de)	1998-01-28
AU5543396A (en)	1996-10-30
AU696516B2 (en)	1998-09-10
NO974740D0 (no)	1997-10-13
DE69637760D1 (de)	2009-01-08
CA2218111A1 (en)	1996-10-17
ATE415411T1 (de)	2008-12-15
NO974740L (no)	1997-12-12
ES2321242T3 (es)	2009-06-03
NZ306782A (en)	1998-11-25
US6207806B1 (en)	2001-03-27
JPH11503733A (ja)	1999-03-30
WO1996032407A1 (en)	1996-10-17
JP3894570B2 (ja)	2007-03-22
US5650496A (en)	1997-07-22

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2016-04-25	MK1K	Patent expired

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