KR900000380A - 활성적인 형태의 단백질 분리방법 - Google Patents
활성적인 형태의 단백질 분리방법 Download PDFInfo
- Publication number
- KR900000380A KR900000380A KR1019880007253A KR880007253A KR900000380A KR 900000380 A KR900000380 A KR 900000380A KR 1019880007253 A KR1019880007253 A KR 1019880007253A KR 880007253 A KR880007253 A KR 880007253A KR 900000380 A KR900000380 A KR 900000380A
- Authority
- KR
- South Korea
- Prior art keywords
- protein
- cation
- cationic
- host cell
- surfactant
- Prior art date
Links
- 238000000164 protein isolation Methods 0.000 title claims 2
- 102000004169 proteins and genes Human genes 0.000 claims abstract 11
- 108090000623 proteins and genes Proteins 0.000 claims abstract 11
- 238000000034 method Methods 0.000 claims abstract 10
- 239000003093 cationic surfactant Substances 0.000 claims abstract 8
- 210000004027 cell Anatomy 0.000 claims 5
- -1 1,1,3,3-tetramethylbutyl Chemical group 0.000 claims 3
- 125000000129 anionic group Chemical group 0.000 claims 3
- 239000003945 anionic surfactant Substances 0.000 claims 3
- 125000002091 cationic group Chemical group 0.000 claims 3
- 238000000926 separation method Methods 0.000 claims 3
- 239000002888 zwitterionic surfactant Substances 0.000 claims 3
- 150000001768 cations Chemical class 0.000 claims 2
- 230000003834 intracellular effect Effects 0.000 claims 2
- FXALIOUHXMVTMJ-UHFFFAOYSA-N CCCCCCCCCCCC([Na])=O Chemical compound CCCCCCCCCCCC([Na])=O FXALIOUHXMVTMJ-UHFFFAOYSA-N 0.000 claims 1
- LZZYPRNAOMGNLH-UHFFFAOYSA-M Cetrimonium bromide Chemical group [Br-].CCCCCCCCCCCCCCCC[N+](C)(C)C LZZYPRNAOMGNLH-UHFFFAOYSA-M 0.000 claims 1
- 102000014150 Interferons Human genes 0.000 claims 1
- 108010050904 Interferons Proteins 0.000 claims 1
- 239000013592 cell lysate Substances 0.000 claims 1
- NEUSVAOJNUQRTM-UHFFFAOYSA-N cetylpyridinium Chemical compound CCCCCCCCCCCCCCCC[N+]1=CC=CC=C1 NEUSVAOJNUQRTM-UHFFFAOYSA-N 0.000 claims 1
- RLGQACBPNDBWTB-UHFFFAOYSA-N cetyltrimethylammonium ion Chemical compound CCCCCCCCCCCCCCCC[N+](C)(C)C RLGQACBPNDBWTB-UHFFFAOYSA-N 0.000 claims 1
- 238000000502 dialysis Methods 0.000 claims 1
- SYELZBGXAIXKHU-UHFFFAOYSA-N dodecyldimethylamine N-oxide Chemical compound CCCCCCCCCCCC[N+](C)(C)[O-] SYELZBGXAIXKHU-UHFFFAOYSA-N 0.000 claims 1
- VICYBMUVWHJEFT-UHFFFAOYSA-N dodecyltrimethylammonium ion Chemical compound CCCCCCCCCCCC[N+](C)(C)C VICYBMUVWHJEFT-UHFFFAOYSA-N 0.000 claims 1
- 238000010828 elution Methods 0.000 claims 1
- 125000001301 ethoxy group Chemical group [H]C([H])([H])C([H])([H])O* 0.000 claims 1
- 125000001495 ethyl group Chemical group [H]C([H])([H])C([H])([H])* 0.000 claims 1
- 238000000855 fermentation Methods 0.000 claims 1
- 230000004151 fermentation Effects 0.000 claims 1
- 239000012530 fluid Substances 0.000 claims 1
- 238000001640 fractional crystallisation Methods 0.000 claims 1
- 239000000122 growth hormone Substances 0.000 claims 1
- 210000003000 inclusion body Anatomy 0.000 claims 1
- 229940047124 interferons Drugs 0.000 claims 1
- 239000003446 ligand Substances 0.000 claims 1
- 230000001926 lymphatic effect Effects 0.000 claims 1
- 239000000693 micelle Substances 0.000 claims 1
- 239000000178 monomer Substances 0.000 claims 1
- 125000000951 phenoxy group Chemical group [H]C1=C([H])C([H])=C(O*)C([H])=C1[H] 0.000 claims 1
- 229920000642 polymer Polymers 0.000 claims 1
- 238000001799 protein solubilization Methods 0.000 claims 1
- 230000007925 protein solubilization Effects 0.000 claims 1
- 150000003839 salts Chemical class 0.000 claims 1
- 159000000000 sodium salts Chemical class 0.000 claims 1
- AMWSQODKOWMURX-UHFFFAOYSA-M sodium;3-[(3-dodecoxy-3-oxopropyl)amino]propanoate Chemical compound [Na+].CCCCCCCCCCCCOC(=O)CCNCCC([O-])=O AMWSQODKOWMURX-UHFFFAOYSA-M 0.000 claims 1
- NPAWNPCNZAPTKA-UHFFFAOYSA-M sodium;propane-1-sulfonate Chemical compound [Na+].CCCS([O-])(=O)=O NPAWNPCNZAPTKA-UHFFFAOYSA-M 0.000 claims 1
- 239000004094 surface-active agent Substances 0.000 claims 1
- GLFDLEXFOHUASB-UHFFFAOYSA-N trimethyl(tetradecyl)azanium Chemical compound CCCCCCCCCCCCCC[N+](C)(C)C GLFDLEXFOHUASB-UHFFFAOYSA-N 0.000 claims 1
- 238000000108 ultra-filtration Methods 0.000 claims 1
- 238000011084 recovery Methods 0.000 abstract 1
- 230000007928 solubilization Effects 0.000 abstract 1
- 238000005063 solubilization Methods 0.000 abstract 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
- C07K1/14—Extraction; Separation; Purification
-
- 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
- C12N1/00—Microorganisms, e.g. protozoa; Compositions thereof; Processes of propagating, maintaining or preserving microorganisms or compositions thereof; Processes of preparing or isolating a composition containing a microorganism; Culture media therefor
- C12N1/06—Lysis of microorganisms
-
- 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
- C07K1/107—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides
- C07K1/113—General methods for the preparation of peptides, i.e. processes for the organic chemical preparation of peptides or proteins of any length by chemical modification of precursor peptides without change of the primary structure
-
- 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
- C07K14/61—Growth hormone [GH], i.e. somatotropin
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biochemistry (AREA)
- Medicinal Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Zoology (AREA)
- Biophysics (AREA)
- Molecular Biology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Wood Science & Technology (AREA)
- Biotechnology (AREA)
- Endocrinology (AREA)
- Analytical Chemistry (AREA)
- General Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Microbiology (AREA)
- Biomedical Technology (AREA)
- Virology (AREA)
- Tropical Medicine & Parasitology (AREA)
- Mycology (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
내용 없음
Description
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음
Claims (10)
- 단백질 분리방법에 있어서, 합성된 발현된 단백질을 포함하는 숙주 세포의 자원 ; 및 최소한 하나의 양이온성, 음이온성 또는 쌍성이온성 계면활성제의 자원을 제공하고 ; 최소한 하나의 양이온성, 음이온성 또는 쌍성이온성 계면활성제를 원하는 단백질 가용화에 충분한 량으로 상기 숙주 세포에 처리하는 과정을 포함함을 특징으로 하는 단백질 분리방법.
- 제1항에 있어서, 합성된 또는 발현된 단백질을 포함하는 숙주 세포를 함유하는 발효액을 제공하고 그로부터 숙주세포를 분리하는 예비 단계를 포함함을 특징으로 하는 단백질 분리방법.
- 제2항에 있어서, 전체적인 세포 용해질을 형성시키기 위하여 숙주 세포를 붕괴시키는 동시 형성단계를 포함함을 특징으로 하는 단백질 분리방법.
- 제1항에 있어서, 합성된 또는 발현된 단백질은 단량체 또는 다량체의 세포내 단백질을 포함함을 특징으로 하는 분리방법.
- 제4항에 있어서, 단량체 또는 다량체의 세포내 단백질은 성장 호르몬, 인터페론, 임뮤노겐, 임파액 또는 그들의 이종 또는 동종 중합체로부터 선택한 봉입체를 포함함을 특징으로 하는 단백질 분리방법.
- 제5항에 있어서, 최소한 하나의 양이온성, 음이온성 또는 쌍성이온성 계면활성체는 약 2.5-5.0 W/V%량으로 존재함을 특징으로 하는 단백질 분리방법.
- 제6항에 있어서, 상게 계면활성제는 다음 양이온중에서 선택한 양이온을 포함하는 양이온 계면활성제임을 특징으로 하는 단백질 분리방법 ; 세틸 트리메틸암모늄 양이온, 세틸 피리디나움 양이온, 테트라데실 트리메틸암모늄 양이온, 도데실 트리메틸암모늄 양이온, 혼합한 n-알킬 디메틸 벤질 암모늄 양이온,,-디메틸,--[2-[2-[4-(1,1,3,3-테트라메틸부틸)페녹시]에톡시]에틸]벤젠메탄아미니움 양이온, 도데실 디메틸아민 산화물,-라우로알사르코신 나트륨 염,-라우로일--메틸라우린 나트륨, 염,-라우릴-이미노디프로피온산 나트륨 염, 3-(,-디메틸 라우릴암모니오)프로판 술폰산 나트륨 염.
- 제7항에 있어서, 양이온성 계면활성제는 세틸 트리 메틸암모늄 브룸화물임을 특징으로 하는 단백질분리방법.
- 제8항에 있어서, 최소한 하나의 양이온 계면활성제는 미셀 농도를 초과하는 량으로 존재함을 특징으로 하는 단백질 분리방법.
- 제6항에 있어서, 생성된 거친 용액으로부터 가융화된 단백질을 분리시키는 분리단계는 크로마토그래피관, 투석, 한외거르기, 분별결정, 또는 리간드 특수 분리를 통한 가용화된 단백질 분별 용리중에서 선택함을 특징으로 하는 단백질 분리방법.※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
Applications Claiming Priority (3)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
AUPI247287 | 1987-06-15 | ||
AUPI12472 | 1987-06-16 | ||
AU?PI2472? | 1987-06-16 |
Publications (2)
Publication Number | Publication Date |
---|---|
KR900000380A true KR900000380A (ko) | 1990-01-30 |
KR0126767B1 KR0126767B1 (ko) | 1997-12-29 |
Family
ID=3772234
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
KR1019880007253A KR0126767B1 (ko) | 1987-06-15 | 1988-06-16 | 계면활성제를 이용한 단백질 회수방법 |
Country Status (14)
Country | Link |
---|---|
US (1) | US4992531A (ko) |
JP (1) | JPS6447389A (ko) |
KR (1) | KR0126767B1 (ko) |
CN (1) | CN1032425C (ko) |
AT (1) | ATE114156T1 (ko) |
AU (1) | AU609824B2 (ko) |
CA (1) | CA1305284C (ko) |
DE (1) | DE3852116T2 (ko) |
DK (1) | DK322188A (ko) |
ES (1) | ES2065911T3 (ko) |
IE (1) | IE66334B1 (ko) |
NO (1) | NO882635L (ko) |
NZ (1) | NZ225032A (ko) |
ZA (1) | ZA884212B (ko) |
Families Citing this family (30)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
AU607988B2 (en) * | 1987-04-21 | 1991-03-21 | Southern Cross Biotech Pty Ltd. | Production of proteins in active forms |
EP0295859B1 (en) * | 1987-06-15 | 1994-11-17 | Southern Cross Biotech Pty.Ltd. | Production of proteins in active forms |
US5102989A (en) * | 1991-03-15 | 1992-04-07 | Merck & Co., Inc. | Method of stabilizing recombinant hepatitis B virus surface proteins from recombinant host cells |
US5252216A (en) * | 1992-03-24 | 1993-10-12 | Smithkline Beecham Corporation | Protein purification |
JPH0774232B2 (ja) * | 1992-08-31 | 1995-08-09 | 農林水産省食品総合研究所長 | 界面活性剤を用いたタンパク質の新規な精製法 |
JP3279362B2 (ja) * | 1992-10-05 | 2002-04-30 | 井上 聰一 | 糖尿病判定方法及び糖尿病判定装置 |
JP3319812B2 (ja) * | 1993-04-05 | 2002-09-03 | 井上 聰一 | リウマチ判定方法及びリウマチ判定装置 |
US20030190307A1 (en) * | 1996-12-24 | 2003-10-09 | Biogen, Inc. | Stable liquid interferon formulations |
US7153943B2 (en) * | 1997-07-14 | 2006-12-26 | Bolder Biotechnology, Inc. | Derivatives of growth hormone and related proteins, and methods of use thereof |
DE69943205D1 (de) | 1998-08-06 | 2011-03-31 | Mountain View Pharmaceuticals | Peg-uricase Konjugate und Verwendung davon |
ATE367398T1 (de) * | 2000-05-16 | 2007-08-15 | Bolder Biotechnology Inc | Verfahren zur rückfaltung von proteinen mit freien cysteinresten |
WO2004027378A2 (en) | 2002-09-20 | 2004-04-01 | Promega Corporation | Luminescence-based methods and probes for measuring cytochrome p450 activity |
WO2004042003A2 (en) * | 2002-11-01 | 2004-05-21 | Promega Corporation | Cell lysis compositions, methods of use, apparatus, and kit |
DE10309691B4 (de) | 2003-02-28 | 2018-10-04 | Hans-Knöll-Institut für Naturstoff-Forschung e.V. | Gewinnung von löslichen Proteinen aus der Biomasse rekombinanter Mikroorganismen |
US20040180445A1 (en) * | 2003-03-12 | 2004-09-16 | Domanico Michael J. | Methods and compositions for purification of nucleic acid from a host cell |
CA2604399A1 (en) | 2005-04-11 | 2006-10-19 | Savient Pharmaceuticals, Inc. | Variant forms of urate oxidase and use thereof |
US9534013B2 (en) * | 2006-04-12 | 2017-01-03 | Horizon Pharma Rheumatology Llc | Purification of proteins with cationic surfactant |
US20080159976A1 (en) * | 2005-04-11 | 2008-07-03 | Jacob Hartman | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
US8148123B2 (en) | 2005-04-11 | 2012-04-03 | Savient Pharmaceuticals, Inc. | Methods for lowering elevated uric acid levels using intravenous injections of PEG-uricase |
CZ2007700A3 (cs) | 2005-04-11 | 2008-02-27 | Savient Pharmaceuticals, Inc. | Variantní forma urátoxidázy a její použití |
WO2006125452A1 (en) * | 2005-05-23 | 2006-11-30 | Universite De Geneve | Injectable superparamagnetic nanoparticles for treatment by hyperthermia and use for forming an hyperthermic implant |
EP2778234B1 (en) | 2005-05-31 | 2017-09-27 | Promega Corporation | Luminogenic and fluorogenic compounds and methods to detect molecules or conditions |
EP2102355B1 (en) | 2006-12-14 | 2016-03-02 | Bolder Biotechnology, Inc. | Long acting proteins and peptides and methods of making and using the same |
US8288559B2 (en) * | 2008-08-18 | 2012-10-16 | Promega Corporation | Luminogenic compounds and methods to detect cytochrome P450 3A enzymes |
GB0901434D0 (en) * | 2009-01-29 | 2009-03-11 | Univ Strathclyde | Ballast water treatment system |
KR101861547B1 (ko) | 2009-06-25 | 2018-07-02 | 크레알타 파마슈티칼스 엘엘씨 | 페길화된 유리카아제 치료 중에 혈청 요산을 모니터링하여 주입 반응의 위험성 및 반응의 항체매개 상실을 예측하는 방법 및 키트 |
CN102905690B (zh) | 2010-05-21 | 2016-03-30 | 西门子医疗保健诊断公司 | 两性离子试剂 |
CN102965317A (zh) * | 2012-11-27 | 2013-03-13 | 江南大学 | 一种产牛磺酸菌株的筛选方法及用该菌株发酵法生产牛磺酸 |
JP6703484B2 (ja) | 2014-01-29 | 2020-06-03 | プロメガ コーポレイションPromega Corporation | 細胞による取り込み測定のための、標識用試薬としての、キノンでマスクされたプローブ |
CN107075544B (zh) * | 2014-07-22 | 2021-01-29 | 生物辐射实验室股份有限公司 | 与聚合酶联用的缓冲液 |
Family Cites Families (6)
Publication number | Priority date | Publication date | Assignee | Title |
---|---|---|---|---|
US4476049A (en) * | 1983-09-20 | 1984-10-09 | Hoffmann-La Roche Inc. | Method for the extraction of immune interferon |
US4677196A (en) * | 1985-09-06 | 1987-06-30 | International Minerals & Chemical Corp. | Purification and activation of proteins from insoluble inclusion bodies |
US4681761A (en) * | 1985-10-24 | 1987-07-21 | State Of Oregon, Acting By And Through The Oregon State Board Of Higher Education, Acting For And On Behalf Of The Oregon Health Sciences University | Major iron-regulated protein of Neisseria gonorrhoeae and its use as vaccine |
AU597924B2 (en) * | 1985-12-11 | 1990-06-14 | Natinco Nv | Solubilization of protein aggregates |
AU612133B2 (en) * | 1987-02-20 | 1991-07-04 | Natinco Nv | Production of proteins in active forms |
AU607988B2 (en) * | 1987-04-21 | 1991-03-21 | Southern Cross Biotech Pty Ltd. | Production of proteins in active forms |
-
1987
- 1987-06-15 AU AU17632/88A patent/AU609824B2/en not_active Ceased
-
1988
- 1988-06-13 ZA ZA884212A patent/ZA884212B/xx unknown
- 1988-06-13 US US07/206,006 patent/US4992531A/en not_active Expired - Fee Related
- 1988-06-14 DK DK322188A patent/DK322188A/da not_active Application Discontinuation
- 1988-06-14 CA CA000569448A patent/CA1305284C/en not_active Expired - Fee Related
- 1988-06-14 ES ES88305404T patent/ES2065911T3/es not_active Expired - Lifetime
- 1988-06-14 DE DE3852116T patent/DE3852116T2/de not_active Expired - Fee Related
- 1988-06-14 AT AT88305404T patent/ATE114156T1/de not_active IP Right Cessation
- 1988-06-15 NO NO882635A patent/NO882635L/no unknown
- 1988-06-15 IE IE181588A patent/IE66334B1/en not_active IP Right Cessation
- 1988-06-15 JP JP63147909A patent/JPS6447389A/ja active Pending
- 1988-06-15 CN CN88103725A patent/CN1032425C/zh not_active Expired - Fee Related
- 1988-06-15 NZ NZ225032A patent/NZ225032A/xx unknown
- 1988-06-16 KR KR1019880007253A patent/KR0126767B1/ko not_active IP Right Cessation
Also Published As
Publication number | Publication date |
---|---|
KR0126767B1 (ko) | 1997-12-29 |
CN1032425C (zh) | 1996-07-31 |
DK322188A (da) | 1988-12-17 |
US4992531A (en) | 1991-02-12 |
AU1763288A (en) | 1988-12-15 |
DE3852116D1 (de) | 1994-12-22 |
ES2065911T3 (es) | 1995-03-01 |
ATE114156T1 (de) | 1994-12-15 |
DK322188D0 (da) | 1988-06-14 |
IE881815L (en) | 1988-12-15 |
CN88103725A (zh) | 1988-12-28 |
NO882635D0 (no) | 1988-06-15 |
DE3852116T2 (de) | 1995-03-30 |
CA1305284C (en) | 1992-07-14 |
NO882635L (no) | 1988-12-19 |
ZA884212B (en) | 1989-03-29 |
AU609824B2 (en) | 1991-05-09 |
JPS6447389A (en) | 1989-02-21 |
IE66334B1 (en) | 1995-12-27 |
NZ225032A (en) | 1991-02-26 |
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