IL91822A - A method for cleansing vitamin K-dependent proteins - Google Patents

A method for cleansing vitamin K-dependent proteins

Info

Publication number: IL91822A
Authority: IL; Israel
Prior art keywords: protein; ion; resin; cation; under conditions
Prior art date: 1988-10-04

Application number

IL9182289A

Other languages

English (en)

Hebrew (he)

Other versions

IL91822A0 (en

Original Assignee

Lilly Co Eli

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.)

1988-10-04

Filing date

1989-09-28

Publication date

2001-06-14

Family has litigation

First worldwide family litigation filed litigation Critical https://patents.darts-ip.com/?family=26943089&utm_source=google_patent&utm_medium=platform_link&utm_campaign=public_patent_search&patent=IL91822(A) "Global patent litigation dataset” by Darts-ip is licensed under a Creative Commons Attribution 4.0 International License.

1989-09-28 Application filed by Lilly Co Eli filed Critical Lilly Co Eli

1990-06-10 Publication of IL91822A0 publication Critical patent/IL91822A0/xx

2001-06-14 Publication of IL91822A publication Critical patent/IL91822A/en

Links

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238000000746 purification Methods 0.000 title description 14
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108090000623 proteins and genes Proteins 0.000 claims abstract description 200
150000001768 cations Chemical class 0.000 claims abstract description 58
239000006143 cell culture medium Substances 0.000 claims abstract description 20
239000000356 contaminant Substances 0.000 claims abstract description 8
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 164
239000011347 resin Substances 0.000 claims description 83
229920005989 resin Polymers 0.000 claims description 83
239000011780 sodium chloride Substances 0.000 claims description 82
101500025568 Homo sapiens Saposin-D Proteins 0.000 claims description 77
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239000000463 material Substances 0.000 claims description 44
230000000694 effects Effects 0.000 claims description 39
230000002209 hydrophobic effect Effects 0.000 claims description 35
NWUYHJFMYQTDRP-UHFFFAOYSA-N 1,2-bis(ethenyl)benzene;1-ethenyl-2-ethylbenzene;styrene Chemical compound C=CC1=CC=CC=C1.CCC1=CC=CC=C1C=C.C=CC1=CC=CC=C1C=C NWUYHJFMYQTDRP-UHFFFAOYSA-N 0.000 claims description 31
238000005342 ion exchange Methods 0.000 claims description 31
239000003456 ion exchange resin Substances 0.000 claims description 31
229920003303 ion-exchange polymer Polymers 0.000 claims description 31
239000011575 calcium Substances 0.000 claims description 25
239000002609 medium Substances 0.000 claims description 22
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 21
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BHPQYMZQTOCNFJ-UHFFFAOYSA-N Calcium cation Chemical compound [Ca+2] BHPQYMZQTOCNFJ-UHFFFAOYSA-N 0.000 claims description 14
-1 anionic amine Chemical class 0.000 claims description 14
239000002158 endotoxin Substances 0.000 claims description 14
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125000001997 phenyl group Chemical group [H]C1=C([H])C([H])=C(*)C([H])=C1[H] 0.000 claims description 13
OYPRJOBELJOOCE-UHFFFAOYSA-N Calcium Chemical compound [Ca] OYPRJOBELJOOCE-UHFFFAOYSA-N 0.000 claims description 12
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SHUZOJHMOBOZST-UHFFFAOYSA-N phylloquinone Natural products CC(C)CCCCC(C)CCC(C)CCCC(=CCC1=C(C)C(=O)c2ccccc2C1=O)C SHUZOJHMOBOZST-UHFFFAOYSA-N 0.000 claims description 4
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CIOAGBVUUVVLOB-UHFFFAOYSA-N strontium atom Chemical compound [Sr] CIOAGBVUUVVLOB-UHFFFAOYSA-N 0.000 claims description 4
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YYLQUHNPNCGKJQ-PIKHSQJKSA-N 3-hydroxy-L-aspartic acid Chemical compound OC(=O)[C@@H](N)C(O)C(O)=O YYLQUHNPNCGKJQ-PIKHSQJKSA-N 0.000 description 3
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TWRXJAOTZQYOKJ-UHFFFAOYSA-L Magnesium chloride Chemical compound [Mg+2].[Cl-].[Cl-] TWRXJAOTZQYOKJ-UHFFFAOYSA-L 0.000 description 3
OKKJLVBELUTLKV-UHFFFAOYSA-N Methanol Chemical compound OC OKKJLVBELUTLKV-UHFFFAOYSA-N 0.000 description 3
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AGVAZMGAQJOSFJ-WZHZPDAFSA-M cobalt(2+);[(2r,3s,4r,5s)-5-(5,6-dimethylbenzimidazol-1-yl)-4-hydroxy-2-(hydroxymethyl)oxolan-3-yl] [(2r)-1-[3-[(1r,2r,3r,4z,7s,9z,12s,13s,14z,17s,18s,19r)-2,13,18-tris(2-amino-2-oxoethyl)-7,12,17-tris(3-amino-3-oxopropyl)-3,5,8,8,13,15,18,19-octamethyl-2 Chemical compound [Co+2].N#[C-].[N-]([C@@H]1[C@H](CC(N)=O)[C@@]2(C)CCC(=O)NC[C@@H](C)OP(O)(=O)O[C@H]3[C@H]([C@H](O[C@@H]3CO)N3C4=CC(C)=C(C)C=C4N=C3)O)\C2=C(C)/C([C@H](C\2(C)C)CCC(N)=O)=N/C/2=C\C([C@H]([C@@]/2(CC(N)=O)C)CCC(N)=O)=N\C\2=C(C)/C2=N[C@]1(C)[C@@](C)(CC(N)=O)[C@@H]2CCC(N)=O AGVAZMGAQJOSFJ-WZHZPDAFSA-M 0.000 description 1
230000000536 complexating effect Effects 0.000 description 1
150000001875 compounds Chemical class 0.000 description 1
230000001143 conditioned effect Effects 0.000 description 1
238000012258 culturing Methods 0.000 description 1
210000000805 cytoplasm Anatomy 0.000 description 1
238000006731 degradation reaction Methods 0.000 description 1
238000011161 development Methods 0.000 description 1
239000012636 effector Substances 0.000 description 1
230000005684 electric field Effects 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
238000011067 equilibration Methods 0.000 description 1
DEFVIWRASFVYLL-UHFFFAOYSA-N ethylene glycol bis(2-aminoethyl)tetraacetic acid Chemical compound OC(=O)CN(CC(O)=O)CCOCCOCCN(CC(O)=O)CC(O)=O DEFVIWRASFVYLL-UHFFFAOYSA-N 0.000 description 1
229960004222 factor ix Drugs 0.000 description 1
230000002349 favourable effect Effects 0.000 description 1
238000002825 functional assay Methods 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
150000002306 glutamic acid derivatives Chemical class 0.000 description 1
108010013113 glutamyl carboxylase Proteins 0.000 description 1
239000008187 granular material Substances 0.000 description 1
230000005484 gravity Effects 0.000 description 1
230000010005 growth-factor like effect Effects 0.000 description 1
230000023597 hemostasis Effects 0.000 description 1
239000012145 high-salt buffer Substances 0.000 description 1
229940099816 human factor vii Drugs 0.000 description 1
229940039715 human prothrombin Drugs 0.000 description 1
229940125396 insulin Drugs 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
239000012540 ion exchange chromatography resin Substances 0.000 description 1
150000002500 ions Chemical class 0.000 description 1
238000010829 isocratic elution Methods 0.000 description 1
210000003292 kidney cell Anatomy 0.000 description 1
229920006008 lipopolysaccharide Polymers 0.000 description 1
239000007788 liquid Substances 0.000 description 1
229920002521 macromolecule Polymers 0.000 description 1
239000011777 magnesium Substances 0.000 description 1
229910001629 magnesium chloride Inorganic materials 0.000 description 1
210000004962 mammalian cell Anatomy 0.000 description 1
102000043253 matrix Gla protein Human genes 0.000 description 1
108010057546 matrix Gla protein Proteins 0.000 description 1
229910052751 metal Inorganic materials 0.000 description 1
239000002184 metal Substances 0.000 description 1
230000003228 microsomal effect Effects 0.000 description 1
238000013508 migration Methods 0.000 description 1
230000005012 migration Effects 0.000 description 1
238000012544 monitoring process Methods 0.000 description 1
238000006386 neutralization reaction Methods 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
229940054441 o-phthalaldehyde Drugs 0.000 description 1
239000008363 phosphate buffer Substances 0.000 description 1
ZWLUXSQADUDCSB-UHFFFAOYSA-N phthalaldehyde Chemical compound O=CC1=CC=CC=C1C=O ZWLUXSQADUDCSB-UHFFFAOYSA-N 0.000 description 1
238000002264 polyacrylamide gel electrophoresis Methods 0.000 description 1
229920001184 polypeptide Polymers 0.000 description 1
230000004481 post-translational protein modification Effects 0.000 description 1
238000002360 preparation method Methods 0.000 description 1
229940039716 prothrombin Drugs 0.000 description 1
239000012266 salt solution Substances 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000001542 size-exclusion chromatography Methods 0.000 description 1
239000011734 sodium Substances 0.000 description 1
238000004611 spectroscopical analysis Methods 0.000 description 1
239000003381 stabilizer Substances 0.000 description 1
239000007858 starting material Substances 0.000 description 1
239000012609 strong anion exchange resin Substances 0.000 description 1
PWYYWQHXAPXYMF-UHFFFAOYSA-N strontium(2+) Chemical compound [Sr+2] PWYYWQHXAPXYMF-UHFFFAOYSA-N 0.000 description 1
239000000126 substance Substances 0.000 description 1
239000006228 supernatant Substances 0.000 description 1
239000013589 supplement Substances 0.000 description 1
238000001890 transfection Methods 0.000 description 1
239000012581 transferrin Substances 0.000 description 1
230000009466 transformation Effects 0.000 description 1
238000005406 washing Methods 0.000 description 1
239000002699 waste material Substances 0.000 description 1
239000003643 water by type Substances 0.000 description 1

Classifications

- C—CHEMISTRY; METALLURGY
- C07—ORGANIC CHEMISTRY
- C07K—PEPTIDES
- C07K1/00—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/647—Blood coagulation factors not provided for in a preceding group or according to more than one of the proceeding groups
- 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
- C07K14/745—Blood coagulation or fibrinolysis factors
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12N—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6478—Aspartic endopeptidases (3.4.23)
- C12N9/6481—Pepsins (3.4.23.1; 3.4.23.2; 3.4.23.3)

Landscapes

Health & Medical Sciences (AREA)
Chemical & Material Sciences (AREA)
Life Sciences & Earth Sciences (AREA)
Organic Chemistry (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biomedical Technology (AREA)
Wood Science & Technology (AREA)
Molecular Biology (AREA)
Medicinal Chemistry (AREA)
General Health & Medical Sciences (AREA)
Biochemistry (AREA)
General Engineering & Computer Science (AREA)
Biotechnology (AREA)
Hematology (AREA)
Microbiology (AREA)
Biophysics (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Toxicology (AREA)
Gastroenterology & Hepatology (AREA)
Analytical Chemistry (AREA)
Peptides Or Proteins (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Micro-Organisms Or Cultivation Processes Thereof (AREA)
Organic Low-Molecular-Weight Compounds And Preparation Thereof (AREA)
Solid-Sorbent Or Filter-Aiding Compositions (AREA)
Enzymes And Modification Thereof (AREA)
Treatment Of Liquids With Adsorbents In General (AREA)

IL9182289A 1988-10-04 1989-09-28 A method for cleansing vitamin K-dependent proteins IL91822A (en)

Applications Claiming Priority (2)

Application Number	Priority Date	Filing Date	Title
US25327988A	1988-10-04	1988-10-04
US07/393,281 US4981952A (en)	1988-10-04	1989-08-16	Method for the purification of vitamin K-dependent proteins

Publications (2)

Publication Number	Publication Date
IL91822A0 IL91822A0 (en)	1990-06-10
IL91822A true IL91822A (en)	2001-06-14

Family

ID=26943089

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL9182289A IL91822A (en)	1988-10-04	1989-09-28	A method for cleansing vitamin K-dependent proteins

Country Status (13)

Country	Link
US (1)	US4981952A (de)
EP (1)	EP0363126B2 (de)
JP (1)	JP2848461B2 (de)
KR (1)	KR0139209B1 (de)
AT (1)	ATE106406T1 (de)
AU (1)	AU635222B2 (de)
CA (1)	CA1314011C (de)
DE (1)	DE68915675T3 (de)
DK (1)	DK176090B1 (de)
ES (1)	ES2054019T5 (de)
HU (1)	HU204538B (de)
IE (1)	IE63765B1 (de)
IL (1)	IL91822A (de)

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CA2410567A1 (en)	2000-05-24	2001-11-29	Eli Lilly And Company	Formulations and use of activated protein c and protein c zymogen for treating hypercoagulable states
CN1250567C (zh) *	2000-07-21	2006-04-12	财团法人化学及血清疗法研究所	钙离子结合蛋白的提纯方法
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US20030055003A1 (en) *	2001-07-19	2003-03-20	David Bar-Or	Use of copper chelators to inhibit the inactivation of protein C
JP4628618B2 (ja) *	2001-09-26	2011-02-09	富士フイルム株式会社	撮像光学系
AU2003213146A1 (en) *	2002-03-08	2003-09-22	Eli Lilly And Company	Activated protein c formulations
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JP2008507561A (ja) *	2004-07-23	2008-03-13	ザユニバーシティオブロチェスター	活性化プロテインｃによる、脳内のプラスミノゲン活性化因子の不都合な作用の阻害
ES2395544T3 (es)	2004-12-23	2013-02-13	Novo Nordisk Health Care Ag	Reducción del contenido de contaminantes proteínicos en composiciones que comprenden una proteína dependiente de la vitamina K de interés
ES2349112T3 (es) *	2005-01-14	2010-12-28	Bayer Healthcare Llc	Método de purificación de factor vii.
ZA200800251B (en) *	2005-06-24	2009-04-29	Drugrecure Aps	Airway administration of tissue factor pathway inhibitor in inflammatory conditions affecting the respiratory track
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EP2004683B1 (de) *	2006-03-24	2016-05-11	Biogen Hemophilia Inc.	Pc5 als faktor-ix-propeptid-verarbeitendes enzym
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1989
- 1989-08-16 US US07/393,281 patent/US4981952A/en not_active Expired - Lifetime
- 1989-09-27 CA CA000613553A patent/CA1314011C/en not_active Expired - Lifetime
- 1989-09-28 IL IL9182289A patent/IL91822A/en not_active IP Right Cessation
- 1989-10-02 ES ES89310061T patent/ES2054019T5/es not_active Expired - Lifetime
- 1989-10-02 DE DE68915675T patent/DE68915675T3/de not_active Expired - Lifetime
- 1989-10-02 AT AT89310061T patent/ATE106406T1/de not_active IP Right Cessation
- 1989-10-02 EP EP89310061A patent/EP0363126B2/de not_active Expired - Lifetime
- 1989-10-03 DK DK198904855A patent/DK176090B1/da not_active IP Right Cessation
- 1989-10-03 HU HU895158A patent/HU204538B/hu not_active IP Right Cessation
- 1989-10-03 IE IE315989A patent/IE63765B1/en not_active IP Right Cessation
- 1989-10-03 JP JP1259873A patent/JP2848461B2/ja not_active Expired - Lifetime
- 1989-10-03 AU AU42519/89A patent/AU635222B2/en not_active Ceased
- 1989-10-04 KR KR1019890014186A patent/KR0139209B1/ko not_active Expired - Fee Related

Also Published As

Publication number	Publication date
DK176090B1 (da)	2006-05-22
ES2054019T5 (es)	2002-10-16
AU635222B2 (en)	1993-03-18
ES2054019T3 (es)	1994-08-01
DE68915675T3 (de)	2002-08-14
JPH02200180A (ja)	1990-08-08
DK485589A (da)	1990-04-05
KR900006511A (ko)	1990-05-08
US4981952A (en)	1991-01-01
JP2848461B2 (ja)	1999-01-20
EP0363126A2 (de)	1990-04-11
AU4251989A (en)	1990-04-12
CA1314011C (en)	1993-03-02
EP0363126B2 (de)	2002-03-06
ATE106406T1 (de)	1994-06-15
IL91822A0 (en)	1990-06-10
EP0363126B1 (de)	1994-06-01
IE63765B1 (en)	1995-06-14
IE893159L (en)	1990-04-04
EP0363126A3 (de)	1991-09-11
KR0139209B1 (ko)	1998-04-30
DE68915675T2 (de)	1994-10-20
DK485589D0 (da)	1989-10-03
HU204538B (en)	1992-01-28
DE68915675D1 (de)	1994-07-07
HUT53373A (en)	1990-10-28

Legal Events

Date	Code	Title
2001-11-25	FF	Patent granted
2002-02-10	KB	Patent renewed
2004-06-01	RH1	Patent not in force

Publication	Publication Date	Title
EP0363126B1 (de)	1994-06-01	Verfahren zur Reinigung von Vitamin K-abhängigen Proteinen
RU2458067C2 (ru)	2012-08-10	Способ выделения плазминогена или плазмина в присутствии фибриногена из смеси
EP4299735B1 (de)	2025-05-21	Verfahren zur reinigung von rekombinantem adamts13 oder anderen proteinen und zusammensetzungen daraus
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