KR960700271A - PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN - Google Patents

PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN

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Publication number
KR960700271A
KR960700271A KR1019950702799A KR19950702799A KR960700271A KR 960700271 A KR960700271 A KR 960700271A KR 1019950702799 A KR1019950702799 A KR 1019950702799A KR 19950702799 A KR19950702799 A KR 19950702799A KR 960700271 A KR960700271 A KR 960700271A
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KR
South Korea
Prior art keywords
glycoprotein
concentration
tris
final
buffer
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KR1019950702799A
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Korean (ko)
Inventor
로버트 엘. 갈릭
스티븐 비. 라일
마이클 와덴
피터 에이. 웰즈
Original Assignee
로렌스 티. 웰츠
디 업존 캄파니
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Application filed by 로렌스 티. 웰츠, 디 업존 캄파니 filed Critical 로렌스 티. 웰츠
Publication of KR960700271A publication Critical patent/KR960700271A/en

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    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
    • C—CHEMISTRY; METALLURGY
    • C07—ORGANIC CHEMISTRY
    • C07K—PEPTIDES
    • C07K14/00—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/005—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from viruses
    • C07K14/08—RNA viruses
    • C07K14/115—Paramyxoviridae, e.g. parainfluenza virus
    • 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
    • C07K1/1136—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 by reversible modification of the secondary, tertiary or quarternary structure, e.g. using denaturating or stabilising agents
    • 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
    • C07K1/34—Extraction; Separation; Purification by filtration, ultrafiltration or reverse osmosis
    • 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
    • C12N2760/00—MICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA ssRNA viruses negative-sense
    • C12N2760/00011—Details
    • C12N2760/18011—Paramyxoviridae
    • C12N2760/18511—Pneumovirus, e.g. human respiratory syncytial virus
    • C12N2760/18522—New viral proteins or individual genes, new structural or functional aspects of known viral proteins or genes

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  • Chemical & Material Sciences (AREA)
  • Organic Chemistry (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Biochemistry (AREA)
  • Biophysics (AREA)
  • General Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Molecular Biology (AREA)
  • Virology (AREA)
  • Analytical Chemistry (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Communicable Diseases (AREA)
  • Crystallography & Structural Chemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • General Chemical & Material Sciences (AREA)
  • Engineering & Computer Science (AREA)
  • Water Supply & Treatment (AREA)
  • Peptides Or Proteins (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)

Abstract

본 발명은 FG 당단백질을 정제시키고 그의 적당한 구조로 리폴딩시키기 위한 방법을 포함한다.The present invention includes methods for purifying FG glycoproteins and refolding them into suitable structures.

Description

인간 호흡계 합포체 바이러스 FG 당단백질의 정제 및 리폴딩 방법(PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN)PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN

본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음As this is a public information case, the full text was not included.

Claims (19)

변성 FG 당단백질을 함유하는 용액을 (a) 요액의 농도를 구아니딘 5.0M 내지 8.0M로 상승시키기 위한 구아니딘, (b) 5 내지 10의 pK가를 갖는 완충제, (c) 적합한 비이온성 또는 쯔비터이온성 세정제 및 (d) 5 내지 10의 pH로 조정한 염기성 용액으로 처리한 후, 투석, 다이아필트레이션(diafiltration) 또는 겔 여과에 의해 구아니딘을 제거함을 포함하는, 적당한 구조로 FG 당단백질을 복원시키기 위한 방법.A solution containing a denatured FG glycoprotein (a) guanidine to raise the concentration of the urine solution to guanidine 5.0M to 8.0M, (b) a buffer having a pK value of 5 to 10, (c) a suitable nonionic or zwitterionic For restoring the FG glycoprotein to a suitable structure, including removing guanidine by treatment with a detergent and (d) a basic solution adjusted to a pH of 5-10, followed by dialysis, diafiltration or gel filtration. Way. 제1항에 있어서, 상기 완충제가 트리스, MES, HEPES 또는 굿(Good) 완충액이고, 상기 적합한 세정제가 비이온성 세정제인 방법.The method of claim 1, wherein the buffer is Tris, MES, HEPES or Good buffer and the suitable cleaner is a nonionic cleaner. 제2항에 있어서, 상기 완충제가 트리스이고, 상기 비이온성 세정제가 n－옥틸 글루코사이드(－옥틸 글루코사이드), 폴리옥시에티렌 에테르(브리즈(Brij)), 폴리옥시에틸렌 소르비탄(트윈(Tween)) 또는 소르비탄(스판(Span))인 방법.3. The method of claim 2 wherein the buffer is Tris and the nonionic detergent is n-octyl glucoside ( -Octyl glucoside), polyoxyethylene ether (Brij), polyoxyethylene sorbitan (Tween) or sorbitan (Span). 제3항에 있어서, 상기 완충제가 트리스이고, 트리스의 농도가 100 내지 300mM이고, 상기 비이온성 세정제가 트윈이고, 트윈 농도가 0.001 내지 20%v/v이고, 최종 pH가 6 내지 9인 방법.The method of claim 3 wherein the buffer is Tris, the concentration of Tris is 100-300 mM, the nonionic detergent is Tween, the Tween concentration is 0.001-20% v / v and the final pH is 6-9. 제1항에 있어서, 최종 pH가 6 내지 9인 방법.The method of claim 1 wherein the final pH is 6-9. 제2항에 있어서, 최종 pH가 6 내지 9인 방법.The method of claim 2 wherein the final pH is 6-9. 제4항에 있어서, 상기 트리스 농도가 약 150mM이고, 상기 트윈 농도가 약 5.0%v/v이고, 최종 pH가 6 내지 8인 방법.The method of claim 4, wherein the Tris concentration is about 150 mM, the twin concentration is about 5.0% v / v, and the final pH is 6-8. (Ⅰ) 역상 충진제 및 희석 산인 이동산 A 및 유기 용매인 이동상 B를 포함하는 역상 크로마토그래피에 의해 FG 당단백질의 용액을 처리하고, (Ⅱ)(a) 상기 용액의 농도를 구아니딘 5.0M 내지 8.0M로 상승시키기 위한 구아니딘, (b) 적합한 완충제, (c) 적합한 세정제 및 (d) 5 내지 10으로 최종 pH를 조정한 염기성 용액을 첨가하므로써 변성 FG 당단백질을 함유하는 용액을 처리한 후, 투석, 다이아필트레이션 또는 겔 여과에 의해 구아니딘을 제거함을 포함하는, 변성 FG 당단백질을 적당한 구조로 복원시킴을 포함하는, 90% 이상의 순도로 FG 당단백질을 정제하기 위한 방법.(I) treating a solution of FG glycoprotein by reverse phase chromatography comprising a reverse phase filler and a mobile acid A as a dilute acid and a mobile phase B as an organic solvent, and (II) (a) adjusting the concentration of the solution to guanidine 5.0M to 8.0 Treatment with a solution containing denatured FG glycoprotein by addition of guanidine to elevate to M, (b) a suitable buffer, (c) a suitable detergent and (d) a basic solution adjusted to a final pH from 5 to 10, followed by dialysis A method for purifying FG glycoproteins with at least 90% purity comprising restoring the modified FG glycoprotein to a suitable structure, including removing guanidine by diafiltration or gel filtration. 제8항에 있어서, 상기 이동상 A가 트리플루오로아세트산이고, 상기 이동상 B가 아세토니트릴인 방법.9. The process of claim 8 wherein said mobile phase A is trifluoroacetic acid and said mobile phase B is acetonitrile. 제9항에 있어서, 상기 완충제가 트리스이고, 상기 적합한 세정제가 트윈이고, 최종 pH가 6 내지 9이고, 상기 이동상 A가 0.01 내지 1%의 농도를 갖는 트리플루오로아세트산인 방법.10. The method of claim 9, wherein the buffer is Tris, the suitable detergent is Tween, the final pH is 6-9, and the mobile phase A is trifluoroacetic acid having a concentration of 0.01-1%. 제10항에 있어서, 상기 트리스의 농도가 100 내지 300mM이고, 상기 트윈 농도가 0.001 내지 20%v/v이고, 최종 pH가 6 내지 9인 방법.The method of claim 10, wherein the concentration of Tris is from 100 to 300 mM, the twin concentration is from 0.001 to 20% v / v, and the final pH is from 6 to 9. 12. 제11항에 있어서, 상기 트리스의 농도가 약 150mM이고, 상기 트윈 농도가 약 5%v/v이고, pH가 7 내지 8인 방법.The method of claim 11, wherein the concentration of Tris is about 150 mM, the tween concentration is about 5% v / v, and the pH is 7-8. 제8항에 있어서, 상기 FG 당단백질을 95%가 넘는 순도로 정제시키는 방법.The method of claim 8, wherein said FG glycoprotein is purified to greater than 95% purity. 제9항에 있어서, 상기 FG 당단백질을 95%가 넘는 순도로 정제시키는 방법.The method of claim 9, wherein said FG glycoprotein is purified to greater than 95% purity. 제10항에 있어서, 상기 FG 당단백질을 95%가 넘는 순도로 정제시키는 방법.The method of claim 10, wherein said FG glycoprotein is purified to greater than 95% purity. 제11항에 있어서, 상기 FG 당단백질을 95%가 넘는 순도로 정제시키는 방법.The method of claim 11, wherein said FG glycoprotein is purified to greater than 95% purity. 제12항에 있어서, 상기 FG 당단백질을 95%가 넘는 순도로 정제시키는 방법.The method of claim 12, wherein said FG glycoprotein is purified to greater than 95% purity. 제1항의 방법에 의해 제조된 당단백질.Glycoprotein prepared by the method of claim 1. 제8항의 방법에 의해 제조된 당단백질.Glycoprotein prepared by the method of claim 8. ※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.※ Note: The disclosure is based on the initial application.
KR1019950702799A 1993-01-08 1993-12-29 PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN KR960700271A (en)

Applications Claiming Priority (3)

Application Number Priority Date Filing Date Title
US187493A 1993-01-08 1993-01-08
US08/001,874 1993-01-08
PCT/US1993/012373 WO1994015968A1 (en) 1993-01-08 1993-12-29 Process for the purification and refolding of human respiratory syncytial virus fg glycoprotein

Publications (1)

Publication Number Publication Date
KR960700271A true KR960700271A (en) 1996-01-19

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KR1019950702799A KR960700271A (en) 1993-01-08 1993-12-29 PROCESS FOR THE PURIFICATION AND REFOLDING OF HUMAN RESPIRATORY SYNCYTIAL VIRUS FG GLYCOPROTEIN

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EP (1) EP0678102A1 (en)
JP (1) JPH08505389A (en)
KR (1) KR960700271A (en)
AU (1) AU5955294A (en)
CA (1) CA2151597A1 (en)
WO (1) WO1994015968A1 (en)

Families Citing this family (6)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
WO1998018819A1 (en) * 1996-10-29 1998-05-07 Smithkline Beecham Biologicals S.A. Purification of respiratory syncytial virus antigens
FR2801219A1 (en) * 2000-09-18 2001-05-25 Pf Medicament Recombinant production of a protein, for particularly use as a carrier protein in nasal vaccines, comprises renaturation, after extraction, in the presence of specific detergents
CA2710600C (en) 2007-12-24 2017-06-06 Id Biomedical Corporation Of Quebec Recombinant rsv antigens
RU2520240C2 (en) * 2008-08-19 2014-06-20 Глитек,Инк. Method of producing glycoprotein and screening method
EA023054B1 (en) 2009-06-24 2016-04-29 Глэксосмитклайн Байолоджикалз С.А. Recombinant rsv antigens
PL3178490T3 (en) 2009-07-15 2022-08-01 Glaxosmithkline Biologicals S.A. Rsv f protein compositions and methods for making same

Family Cites Families (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
KR0137963B1 (en) * 1987-12-23 1998-04-30 로버트 에이. 아미테이지 Chimeric glycoproteins containing immunogenic segments of the glyocoproteins of human respiratory syncytial virus
GB8927546D0 (en) * 1989-12-06 1990-02-07 Ciba Geigy Process for the production of biologically active tgf-beta

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EP0678102A1 (en) 1995-10-25
CA2151597A1 (en) 1994-07-21
JPH08505389A (en) 1996-06-11
AU5955294A (en) 1994-08-15
WO1994015968A1 (en) 1994-07-21

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