TW206236B - - Google Patents

Download PDF

Info

Publication number: TW206236B
Authority: TW; Taiwan
Prior art keywords: pro; protein; seq; glu; arg
Prior art date: 1991-02-21

Application number

TW81101114A

Other languages

English (en)

Chinese (zh)

Original Assignee

Boehringer Mannheim Gmbh

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.)

1991-02-21

Filing date

1992-02-17

Publication date

1993-05-21

1992-02-17 Application filed by Boehringer Mannheim Gmbh filed Critical Boehringer Mannheim Gmbh

1993-05-21 Application granted granted Critical

1993-05-21 Publication of TW206236B publication Critical patent/TW206236B/zh

Links

108090000623 proteins and genes Proteins 0.000 claims description 45
235000018102 proteins Nutrition 0.000 claims description 39
102000004169 proteins and genes Human genes 0.000 claims description 39
238000000034 method Methods 0.000 claims description 30
235000001014 amino acid Nutrition 0.000 claims description 25
150000001413 amino acids Chemical class 0.000 claims description 25
239000002253 acid Substances 0.000 claims description 18
102000007056 Recombinant Fusion Proteins Human genes 0.000 claims description 17
108010008281 Recombinant Fusion Proteins Proteins 0.000 claims description 17
150000001412 amines Chemical class 0.000 claims description 17
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 13
239000004475 Arginine Substances 0.000 claims description 10
235000009697 arginine Nutrition 0.000 claims description 10
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 10
238000004153 renaturation Methods 0.000 claims description 10
230000004913 activation Effects 0.000 claims description 7
KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 claims description 6
235000013922 glutamic acid Nutrition 0.000 claims description 6
239000004220 glutamic acid Substances 0.000 claims description 6
WHUUTDBJXJRKMK-UHFFFAOYSA-N Glutamic acid Natural products OC(=O)C(N)CCC(O)=O WHUUTDBJXJRKMK-UHFFFAOYSA-N 0.000 claims description 5
WHUUTDBJXJRKMK-VKHMYHEASA-N L-glutamic acid Chemical compound OC(=O)[C@@H](N)CCC(O)=O WHUUTDBJXJRKMK-VKHMYHEASA-N 0.000 claims description 5
CKLJMWTZIZZHCS-REOHCLBHSA-N L-aspartic acid Chemical compound OC(=O)[C@@H](N)CC(O)=O CKLJMWTZIZZHCS-REOHCLBHSA-N 0.000 claims description 4
KDXKERNSBIXSRK-YFKPBYRVSA-N L-lysine Chemical compound NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 4
239000004472 Lysine Substances 0.000 claims description 4
235000003704 aspartic acid Nutrition 0.000 claims description 4
OQFSQFPPLPISGP-UHFFFAOYSA-N beta-carboxyaspartic acid Natural products OC(=O)C(N)C(C(O)=O)C(O)=O OQFSQFPPLPISGP-UHFFFAOYSA-N 0.000 claims description 4
125000000291 glutamic acid group Chemical group N[C@@H](CCC(O)=O)C(=O)* 0.000 claims description 4
235000018977 lysine Nutrition 0.000 claims description 4
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims description 3
108091005804 Peptidases Proteins 0.000 claims description 3
239000004365 Protease Substances 0.000 claims description 3
102100037486 Reverse transcriptase/ribonuclease H Human genes 0.000 claims description 3
230000003213 activating effect Effects 0.000 claims description 3
238000011049 filling Methods 0.000 claims description 3
YCYXHLZRUSJITQ-SRVKXCTJSA-N Arg-Pro-Pro Chemical compound NC(=N)NCCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N1[C@H](C(O)=O)CCC1 YCYXHLZRUSJITQ-SRVKXCTJSA-N 0.000 claims description 2
108010074860 Factor Xa Proteins 0.000 claims description 2
ADHNYKZHPOEULM-BQBZGAKWSA-N Met-Glu Chemical compound CSCC[C@H](N)C(=O)N[C@H](C(O)=O)CCC(O)=O ADHNYKZHPOEULM-BQBZGAKWSA-N 0.000 claims description 2
ONIBWKKTOPOVIA-UHFFFAOYSA-N Proline Natural products OC(=O)C1CCCN1 ONIBWKKTOPOVIA-UHFFFAOYSA-N 0.000 claims description 2
108010029539 arginyl-prolyl-proline Proteins 0.000 claims description 2
230000001976 improved effect Effects 0.000 claims description 2
108010056582 methionylglutamic acid Proteins 0.000 claims description 2
235000013930 proline Nutrition 0.000 claims description 2
239000000126 substance Substances 0.000 claims description 2
125000003277 amino group Chemical group 0.000 claims 2
125000003178 carboxy group Chemical group [H]OC(*)=O 0.000 claims 2
FWMNVWWHGCHHJJ-SKKKGAJSSA-N 4-amino-1-[(2r)-6-amino-2-[[(2r)-2-[[(2r)-2-[[(2r)-2-amino-3-phenylpropanoyl]amino]-3-phenylpropanoyl]amino]-4-methylpentanoyl]amino]hexanoyl]piperidine-4-carboxylic acid Chemical compound C([C@H](C(=O)N[C@H](CC(C)C)C(=O)N[C@H](CCCCN)C(=O)N1CCC(N)(CC1)C(O)=O)NC(=O)[C@H](N)CC=1C=CC=CC=1)C1=CC=CC=C1 FWMNVWWHGCHHJJ-SKKKGAJSSA-N 0.000 claims 1
102000004269 Granulocyte Colony-Stimulating Factor Human genes 0.000 claims 1
108010017080 Granulocyte Colony-Stimulating Factor Proteins 0.000 claims 1
241000237988 Patellidae Species 0.000 claims 1
230000004936 stimulating effect Effects 0.000 claims 1
229940024606 amino acid Drugs 0.000 description 20
210000004027 cell Anatomy 0.000 description 17
239000000872 buffer Substances 0.000 description 11
238000006243 chemical reaction Methods 0.000 description 10
229960003121 arginine Drugs 0.000 description 9
238000000502 dialysis Methods 0.000 description 9
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 description 8
230000007420 reactivation Effects 0.000 description 8
108091034117 Oligonucleotide Proteins 0.000 description 7
239000007983 Tris buffer Substances 0.000 description 7
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 7
LFQSCWFLJHTTHZ-UHFFFAOYSA-N Ethanol Chemical compound CCO LFQSCWFLJHTTHZ-UHFFFAOYSA-N 0.000 description 6
210000003000 inclusion body Anatomy 0.000 description 6
239000000243 solution Substances 0.000 description 6
230000000694 effects Effects 0.000 description 5
235000012054 meals Nutrition 0.000 description 4
239000000203 mixture Substances 0.000 description 4
210000001236 prokaryotic cell Anatomy 0.000 description 4
KWTQSFXGGICVPE-UHFFFAOYSA-N 2-amino-5-(diaminomethylideneamino)pentanoic acid;hydron;chloride Chemical compound Cl.OC(=O)C(N)CCCN=C(N)N KWTQSFXGGICVPE-UHFFFAOYSA-N 0.000 description 3
WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 3
108020004414 DNA Proteins 0.000 description 3
108010053070 Glutathione Disulfide Proteins 0.000 description 3
QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 3
108091028043 Nucleic acid sequence Proteins 0.000 description 3
JLCPHMBAVCMARE-UHFFFAOYSA-N [3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[3-[[3-[[3-[[3-[[3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-[[5-(2-amino-6-oxo-1H-purin-9-yl)-3-hydroxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxyoxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(5-methyl-2,4-dioxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(6-aminopurin-9-yl)oxolan-2-yl]methoxy-hydroxyphosphoryl]oxy-5-(4-amino-2-oxopyrimidin-1-yl)oxolan-2-yl]methyl [5-(6-aminopurin-9-yl)-2-(hydroxymethyl)oxolan-3-yl] hydrogen phosphate Polymers Cc1cn(C2CC(OP(O)(=O)OCC3OC(CC3OP(O)(=O)OCC3OC(CC3O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c3nc(N)[nH]c4=O)C(COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3COP(O)(=O)OC3CC(OC3CO)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3ccc(N)nc3=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cc(C)c(=O)[nH]c3=O)n3cc(C)c(=O)[nH]c3=O)n3ccc(N)nc3=O)n3cc(C)c(=O)[nH]c3=O)n3cnc4c3nc(N)[nH]c4=O)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)n3cnc4c(N)ncnc34)O2)c(=O)[nH]c1=O JLCPHMBAVCMARE-UHFFFAOYSA-N 0.000 description 3
235000004279 alanine Nutrition 0.000 description 3
238000004458 analytical method Methods 0.000 description 3
238000005119 centrifugation Methods 0.000 description 3
239000012634 fragment Substances 0.000 description 3
YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 3
229960000789 guanidine hydrochloride Drugs 0.000 description 3
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 3
238000004128 high performance liquid chromatography Methods 0.000 description 3
230000020477 pH reduction Effects 0.000 description 3
210000002706 plastid Anatomy 0.000 description 3
238000002360 preparation method Methods 0.000 description 3
238000005063 solubilization Methods 0.000 description 3
230000007928 solubilization Effects 0.000 description 3
238000002604 ultrasonography Methods 0.000 description 3
HVBSAKJJOYLTQU-UHFFFAOYSA-N 4-aminobenzenesulfonic acid Chemical compound NC1=CC=C(S(O)(=O)=O)C=C1 HVBSAKJJOYLTQU-UHFFFAOYSA-N 0.000 description 2
QGZKDVFQNNGYKY-UHFFFAOYSA-N Ammonia Chemical compound N QGZKDVFQNNGYKY-UHFFFAOYSA-N 0.000 description 2
241000894006 Bacteria Species 0.000 description 2
ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 description 2
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 2
ROHFNLRQFUQHCH-YFKPBYRVSA-N L-leucine Chemical compound CC(C)C[C@H](N)C(O)=O ROHFNLRQFUQHCH-YFKPBYRVSA-N 0.000 description 2
ROHFNLRQFUQHCH-UHFFFAOYSA-N Leucine Natural products CC(C)CC(N)C(O)=O ROHFNLRQFUQHCH-UHFFFAOYSA-N 0.000 description 2
UCKMPCXJQFINFW-UHFFFAOYSA-N Sulphide Chemical compound [S-2] UCKMPCXJQFINFW-UHFFFAOYSA-N 0.000 description 2
DTQVDTLACAAQTR-UHFFFAOYSA-N Trifluoroacetic acid Chemical compound OC(=O)C(F)(F)F DTQVDTLACAAQTR-UHFFFAOYSA-N 0.000 description 2
230000033228 biological regulation Effects 0.000 description 2
230000002079 cooperative effect Effects 0.000 description 2
230000001419 dependent effect Effects 0.000 description 2
239000000284 extract Substances 0.000 description 2
235000013305 food Nutrition 0.000 description 2
ZDXPYRJPNDTMRX-UHFFFAOYSA-N glutamine Natural products OC(=O)C(N)CCC(N)=O ZDXPYRJPNDTMRX-UHFFFAOYSA-N 0.000 description 2
235000005772 leucine Nutrition 0.000 description 2
239000002609 medium Substances 0.000 description 2
239000012454 non-polar solvent Substances 0.000 description 2
230000035755 proliferation Effects 0.000 description 2
ODLMAHJVESYWTB-UHFFFAOYSA-N propylbenzene Chemical compound CCCC1=CC=CC=C1 ODLMAHJVESYWTB-UHFFFAOYSA-N 0.000 description 2
239000005871 repellent Substances 0.000 description 2
239000011537 solubilization buffer Substances 0.000 description 2
239000007858 starting material Substances 0.000 description 2
230000001225 therapeutic effect Effects 0.000 description 2
229940104230 thymidine Drugs 0.000 description 2
101150084750 1 gene Proteins 0.000 description 1
RYHBNJHYFVUHQT-UHFFFAOYSA-N 1,4-Dioxane Chemical compound C1COCCO1 RYHBNJHYFVUHQT-UHFFFAOYSA-N 0.000 description 1
108010011485 Aspartame Proteins 0.000 description 1
102000040350 B family Human genes 0.000 description 1
108091072128 B family Proteins 0.000 description 1
102000007644 Colony-Stimulating Factors Human genes 0.000 description 1
108010071942 Colony-Stimulating Factors Proteins 0.000 description 1
102000010970 Connexin Human genes 0.000 description 1
108050001175 Connexin Proteins 0.000 description 1
XFXPMWWXUTWYJX-UHFFFAOYSA-N Cyanide Chemical compound N#[C-] XFXPMWWXUTWYJX-UHFFFAOYSA-N 0.000 description 1
238000001712 DNA sequencing Methods 0.000 description 1
102000016911 Deoxyribonucleases Human genes 0.000 description 1
108010053770 Deoxyribonucleases Proteins 0.000 description 1
241000588724 Escherichia coli Species 0.000 description 1
241001131785 Escherichia coli HB101 Species 0.000 description 1
102000003839 Human Proteins Human genes 0.000 description 1
108090000144 Human Proteins Proteins 0.000 description 1
DGAQECJNVWCQMB-PUAWFVPOSA-M Ilexoside XXIX Chemical compound C[C@@H]1CC[C@@]2(CC[C@@]3(C(=CC[C@H]4[C@]3(CC[C@@H]5[C@@]4(CC[C@@H](C5(C)C)OS(=O)(=O)[O-])C)C)[C@@H]2[C@]1(C)O)C)C(=O)O[C@H]6[C@@H]([C@H]([C@@H]([C@H](O6)CO)O)O)O.[Na+] DGAQECJNVWCQMB-PUAWFVPOSA-M 0.000 description 1
102000014150 Interferons Human genes 0.000 description 1
108010050904 Interferons Proteins 0.000 description 1
102000015696 Interleukins Human genes 0.000 description 1
108010063738 Interleukins Proteins 0.000 description 1
ONIBWKKTOPOVIA-BYPYZUCNSA-N L-Proline Chemical compound OC(=O)[C@@H]1CCCN1 ONIBWKKTOPOVIA-BYPYZUCNSA-N 0.000 description 1
FFEARJCKVFRZRR-BYPYZUCNSA-N L-methionine Chemical compound CSCC[C@H](N)C(O)=O FFEARJCKVFRZRR-BYPYZUCNSA-N 0.000 description 1
FYYHWMGAXLPEAU-UHFFFAOYSA-N Magnesium Chemical compound [Mg] FYYHWMGAXLPEAU-UHFFFAOYSA-N 0.000 description 1
102000016943 Muramidase Human genes 0.000 description 1
108010014251 Muramidase Proteins 0.000 description 1
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 description 1
240000002853 Nelumbo nucifera Species 0.000 description 1
235000006508 Nelumbo nucifera Nutrition 0.000 description 1
235000006510 Nelumbo pentapetala Nutrition 0.000 description 1
MCWHYUWXVNRXFV-RWMBFGLXSA-N Pro-Leu-Pro Chemical compound CC(C)C[C@@H](C(=O)N1CCC[C@@H]1C(=O)O)NC(=O)[C@@H]2CCCN2 MCWHYUWXVNRXFV-RWMBFGLXSA-N 0.000 description 1
102000057361 Pseudogenes Human genes 0.000 description 1
108091008109 Pseudogenes Proteins 0.000 description 1
239000012979 RPMI medium Substances 0.000 description 1
206010065954 Stubbornness Diseases 0.000 description 1
JZRWCGZRTZMZEH-UHFFFAOYSA-N Thiamine Natural products CC1=C(CCO)SC=[N+]1CC1=CN=C(C)N=C1N JZRWCGZRTZMZEH-UHFFFAOYSA-N 0.000 description 1
229920004890 Triton X-100 Polymers 0.000 description 1
230000002378 acidificating effect Effects 0.000 description 1
239000012190 activator Substances 0.000 description 1
125000000539 amino acid group Chemical group 0.000 description 1
229910021529 ammonia Inorganic materials 0.000 description 1
AVKUERGKIZMTKX-NJBDSQKTSA-N ampicillin Chemical compound C1([C@@H](N)C(=O)N[C@H]2[C@H]3SC([C@@H](N3C2=O)C(O)=O)(C)C)=CC=CC=C1 AVKUERGKIZMTKX-NJBDSQKTSA-N 0.000 description 1
229960000723 ampicillin Drugs 0.000 description 1
230000003698 anagen phase Effects 0.000 description 1
230000002882 anti-plaque Effects 0.000 description 1
IAOZJIPTCAWIRG-QWRGUYRKSA-N aspartame Chemical compound OC(=O)C[C@H](N)C(=O)N[C@H](C(=O)OC)CC1=CC=CC=C1 IAOZJIPTCAWIRG-QWRGUYRKSA-N 0.000 description 1
239000000605 aspartame Substances 0.000 description 1
229960003438 aspartame Drugs 0.000 description 1
235000010357 aspartame Nutrition 0.000 description 1
210000004899 c-terminal region Anatomy 0.000 description 1
244000309466 calf Species 0.000 description 1
239000004202 carbamide Substances 0.000 description 1
239000013592 cell lysate Substances 0.000 description 1
230000008859 change Effects 0.000 description 1
239000003795 chemical substances by application Substances 0.000 description 1
238000003776 cleavage reaction Methods 0.000 description 1
229940047120 colony stimulating factors Drugs 0.000 description 1
238000010411 cooking Methods 0.000 description 1
239000000385 dialysis solution Substances 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
238000004090 dissolution Methods 0.000 description 1
101150097231 eg gene Proteins 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
238000000855 fermentation Methods 0.000 description 1
230000004151 fermentation Effects 0.000 description 1
238000009472 formulation Methods 0.000 description 1
230000002068 genetic effect Effects 0.000 description 1
239000003365 glass fiber Substances 0.000 description 1
WHUUTDBJXJRKMK-VKHMYHEASA-L glutamate group Chemical group N[C@@H](CCC(=O)[O-])C(=O)[O-] WHUUTDBJXJRKMK-VKHMYHEASA-L 0.000 description 1
150000002307 glutamic acids Chemical class 0.000 description 1
PCHJSUWPFVWCPO-UHFFFAOYSA-N gold Chemical compound [Au] PCHJSUWPFVWCPO-UHFFFAOYSA-N 0.000 description 1
239000010931 gold Substances 0.000 description 1
229910052737 gold Inorganic materials 0.000 description 1
210000003714 granulocyte Anatomy 0.000 description 1
229960004198 guanidine Drugs 0.000 description 1
230000002209 hydrophobic effect Effects 0.000 description 1
230000006872 improvement Effects 0.000 description 1
238000011534 incubation Methods 0.000 description 1
230000001939 inductive effect Effects 0.000 description 1
238000009434 installation Methods 0.000 description 1
229940079322 interferon Drugs 0.000 description 1
229940047122 interleukins Drugs 0.000 description 1
BPHPUYQFMNQIOC-NXRLNHOXSA-N isopropyl beta-D-thiogalactopyranoside Chemical compound CC(C)S[C@@H]1O[C@H](CO)[C@H](O)[C@H](O)[C@H]1O BPHPUYQFMNQIOC-NXRLNHOXSA-N 0.000 description 1
229930027917 kanamycin Natural products 0.000 description 1
229960000318 kanamycin Drugs 0.000 description 1
SBUJHOSQTJFQJX-NOAMYHISSA-N kanamycin Chemical compound O[C@@H]1[C@@H](O)[C@H](O)[C@@H](CN)O[C@@H]1O[C@H]1[C@H](O)[C@@H](O[C@@H]2[C@@H]([C@@H](N)[C@H](O)[C@@H](CO)O2)O)[C@H](N)C[C@@H]1N SBUJHOSQTJFQJX-NOAMYHISSA-N 0.000 description 1
229930182823 kanamycin A Natural products 0.000 description 1
208000032839 leukemia Diseases 0.000 description 1
210000004072 lung Anatomy 0.000 description 1
239000004325 lysozyme Substances 0.000 description 1
229960000274 lysozyme Drugs 0.000 description 1
235000010335 lysozyme Nutrition 0.000 description 1
239000011777 magnesium Substances 0.000 description 1
229910052749 magnesium Inorganic materials 0.000 description 1
238000005259 measurement Methods 0.000 description 1
229930182817 methionine Natural products 0.000 description 1
230000004048 modification Effects 0.000 description 1
238000012986 modification Methods 0.000 description 1
239000013612 plasmid Substances 0.000 description 1
125000002924 primary amino group Chemical group [H]N([H])* 0.000 description 1
239000006041 probiotic Substances 0.000 description 1
230000000529 probiotic effect Effects 0.000 description 1
235000018291 probiotics Nutrition 0.000 description 1
230000007026 protein scission Effects 0.000 description 1
230000003252 repetitive effect Effects 0.000 description 1
230000007017 scission Effects 0.000 description 1
210000002966 serum Anatomy 0.000 description 1
239000011734 sodium Substances 0.000 description 1
229910052708 sodium Inorganic materials 0.000 description 1
239000002904 solvent Substances 0.000 description 1
229950000244 sulfanilic acid Drugs 0.000 description 1
239000000725 suspension Substances 0.000 description 1
238000010998 test method Methods 0.000 description 1
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 1
KYMBYSLLVAOCFI-UHFFFAOYSA-N thiamine Chemical compound CC1=C(CCO)SCN1CC1=CN=C(C)N=C1N KYMBYSLLVAOCFI-UHFFFAOYSA-N 0.000 description 1
235000019157 thiamine Nutrition 0.000 description 1
229960003495 thiamine Drugs 0.000 description 1
239000011721 thiamine Substances 0.000 description 1
-1 tyrosin aldehyde Chemical class 0.000 description 1
OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
150000003672 ureas Chemical class 0.000 description 1

Landscapes

Peptides Or Proteins (AREA)

TW81101114A 1991-02-21 1992-02-17 TW206236B (fr)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
DE4165480		1991-02-21

Publications (1)

Publication Number	Publication Date
TW206236B true TW206236B (fr)	1993-05-21

Family

ID=51356767

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
TW81101114A TW206236B (fr)	1991-02-21	1992-02-17

Country Status (1)

Country	Link
TW (1)	TW206236B (fr)

1992
- 1992-02-17 TW TW81101114A patent/TW206236B/zh active

Publication	Publication Date	Title
JP2686090B2 (ja)	1997-12-08	新規融合蛋白質およびその精製方法
EP0155549B1 (fr)	1991-03-20	ADN codant pour le facteur humain de nécrose de tumeur et le polypeptide du facteur humain de nécrose de tumeur
FI106029B (fi)	2000-11-15	Yhdistelmä -DNA-teknisten proteiinien parannettu aktivointi
EP0751220A1 (fr)	1997-01-02	Protéine hautement purifiée, sa production et utilisation
CN106434717A (zh)	2017-02-22	一种生物合成制备人glp‑1多肽或其类似物的方法
HU197349B (en)	1989-03-28	Process for producing cloning vectors usable for the expression of growth hormones
CN105473609A (zh)	2016-04-06	用于表达肽和蛋白的方法
RU2144957C1 (ru)	2000-01-27	РЕКОМБИНАНТНАЯ ПЛАЗМИДНАЯ ДНК pPINS07, КОДИРУЮЩАЯ ГИБРИДНЫЙ ПОЛИПЕПТИД, СОДЕРЖАЩИЙ ПРОИНСУЛИН ЧЕЛОВЕКА, И ШТАММ БАКТЕРИЙ Escherichia coli - ПРОДУЦЕНТ ГИБРИДНОГО ПОЛИПЕПТИДА, СОДЕРЖАЩЕГО ПРОИНСУЛИН ЧЕЛОВЕКА
EP1924601B1 (fr)	2011-10-19	Expression protéique dans e.coli
JP5347255B2 (ja)	2013-11-20	組換え蛋白質の可溶性蛋白質としての製造方法
CN1230542C (zh)	2005-12-07	通过自我蛋白水解生产蛋白质
Tomisawa et al.	2015	Efficient production of a correctly folded mouse α-defensin, cryptdin-4, by refolding during inclusion body solubilization
KR101373297B1 (ko)	2014-03-11	대장균 포스포글리세르산 인산화효소 유전자를 융합 파트너로서 포함하는 발현벡터
TW206236B (fr)	1993-05-21
CN101622269A (zh)	2010-01-06	蛋白质在大肠杆菌中的表达
JP2549504B2 (ja)	1996-10-30	Ｄｎａ塩基配列、ポリペプチド分泌発現ベクター及び形質転換微生物
KR100890184B1 (ko)	2009-03-25	ＳｌｙＤ를 융합파트너로 이용한 재조합 단백질의 제조방법
RU2610173C1 (ru)	2017-02-08	Рекомбинантная плазмида pFM-IFN-17, обеспечивающая экспрессию интерферона альфа-2b человека, рекомбинантная плазмида pFM-АР, обеспечивающая экспрессию фермента метионинаминопептидазы E. coli, биплазмидный штамм Escherichia coli FM-IFN-АР (pFM-IFN-17, pFM-АР) - продуцент (Met-) рекомбинантного интерферона альфа-2b человека
KR100890187B1 (ko)	2009-03-25	Ｔｓｆ를 융합파트너로 이용한 재조합 단백질의 제조방법
KR100890183B1 (ko)	2009-03-25	말산탈수소효소를 융합파트너로 이용한 재조합 단백질의제조방법
CN104136460A (zh)	2014-11-05	减少1->3读框移位的方法
JP2602067B2 (ja)	1997-04-23	ヒラメ成長ホルモン、ヒラメ成長ホルモン構造遺伝子、ヒラメ成長ホルモン生産用組換えプラスミド、ヒラメプレ成長ホルモン、ヒラメプレ成長ホルモン構造遺伝子、ヒラメプレ成長構造遺伝子組換えプラスミド、ヒラメ成長ホルモン及びヒラメプレ成長ホルモンの製造方法
CN104136459A (zh)	2014-11-05	减少1-＞2读框移位的方法
JPH0928380A (ja)	1997-02-04	ニトリラーゼ遺伝子発現に関わる調節因子およびその遺伝子
KR100890188B1 (ko)	2009-03-25	ＰｏｔＤ를 융합파트너로 이용한 재조합 단백질의 제조방법