KR850003734A - 고 정제 단백질의 제조방법 - Google Patents
고 정제 단백질의 제조방법 Download PDFInfo
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- KR850003734A KR850003734A KR1019840007430A KR840007430A KR850003734A KR 850003734 A KR850003734 A KR 850003734A KR 1019840007430 A KR1019840007430 A KR 1019840007430A KR 840007430 A KR840007430 A KR 840007430A KR 850003734 A KR850003734 A KR 850003734A
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- 238000000034 method Methods 0.000 title claims 10
- 102000004169 proteins and genes Human genes 0.000 title claims 5
- 108090000623 proteins and genes Proteins 0.000 title claims 5
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 claims description 10
- 102000055277 human IL2 Human genes 0.000 claims description 10
- 230000000694 effects Effects 0.000 claims description 3
- 102000000588 Interleukin-2 Human genes 0.000 claims description 2
- 108010002350 Interleukin-2 Proteins 0.000 claims description 2
- 238000004587 chromatography analysis Methods 0.000 claims 3
- IVGJYOOGJLFKQE-AVGNSLFASA-N Glu-Leu-Lys Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CCCCN)C(=O)O)NC(=O)[C@H](CCC(=O)O)N IVGJYOOGJLFKQE-AVGNSLFASA-N 0.000 claims 2
- 230000002209 hydrophobic effect Effects 0.000 claims 2
- 239000007788 liquid Substances 0.000 claims 2
- 238000002360 preparation method Methods 0.000 claims 2
- CNKBMTKICGGSCQ-ACRUOGEOSA-N (2S)-2-[[(2S)-2-[[(2S)-2,6-diamino-1-oxohexyl]amino]-1-oxo-3-phenylpropyl]amino]-3-(4-hydroxyphenyl)propanoic acid Chemical compound C([C@H](NC(=O)[C@@H](N)CCCCN)C(=O)N[C@@H](CC=1C=CC(O)=CC=1)C(O)=O)C1=CC=CC=C1 CNKBMTKICGGSCQ-ACRUOGEOSA-N 0.000 claims 1
- OTCJMMRQBVDQRK-DCAQKATOSA-N Arg-Asp-Leu Chemical compound [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O OTCJMMRQBVDQRK-DCAQKATOSA-N 0.000 claims 1
- CQMQJWRCRQSBAF-BPUTZDHNSA-N Asn-Arg-Trp Chemical compound C1=CC=C2C(=C1)C(=CN2)C[C@@H](C(=O)O)NC(=O)[C@H](CCCN=C(N)N)NC(=O)[C@H](CC(=O)N)N CQMQJWRCRQSBAF-BPUTZDHNSA-N 0.000 claims 1
- PNHQRQTVBRDIEF-CIUDSAMLSA-N Asn-Leu-Ala Chemical compound C[C@@H](C(=O)O)NC(=O)[C@H](CC(C)C)NC(=O)[C@H](CC(=O)N)N PNHQRQTVBRDIEF-CIUDSAMLSA-N 0.000 claims 1
- BKZFBJYIVSBXCO-KKUMJFAQSA-N Asn-Phe-His Chemical compound [H]N[C@@H](CC(N)=O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)N[C@@H](CC1=CNC=N1)C(O)=O BKZFBJYIVSBXCO-KKUMJFAQSA-N 0.000 claims 1
- HHABWQIFXZPZCK-ACZMJKKPSA-N Cys-Gln-Ser Chemical compound C(CC(=O)N)[C@@H](C(=O)N[C@@H](CO)C(=O)O)NC(=O)[C@H](CS)N HHABWQIFXZPZCK-ACZMJKKPSA-N 0.000 claims 1
- XLLSMEFANRROJE-GUBZILKMSA-N Cys-Leu-Glu Chemical compound CC(C)C[C@@H](C(=O)N[C@@H](CCC(=O)O)C(=O)O)NC(=O)[C@H](CS)N XLLSMEFANRROJE-GUBZILKMSA-N 0.000 claims 1
- QKCZZAZNMMVICF-DCAQKATOSA-N Gln-Leu-Glu Chemical compound NC(=O)CC[C@H](N)C(=O)N[C@@H](CC(C)C)C(=O)N[C@@H](CCC(O)=O)C(O)=O QKCZZAZNMMVICF-DCAQKATOSA-N 0.000 claims 1
- DOMHVQBSRJNNKD-ZPFDUUQYSA-N Gln-Met-Ile Chemical compound [H]N[C@@H](CCC(N)=O)C(=O)N[C@@H](CCSC)C(=O)N[C@@H]([C@@H](C)CC)C(O)=O DOMHVQBSRJNNKD-ZPFDUUQYSA-N 0.000 claims 1
- KPNWAJMEMRCLAL-GUBZILKMSA-N Gln-Ser-Lys Chemical compound C(CCN)C[C@@H](C(=O)O)NC(=O)[C@H](CO)NC(=O)[C@H](CCC(=O)N)N KPNWAJMEMRCLAL-GUBZILKMSA-N 0.000 claims 1
- MUSGDMDGNGXULI-DCAQKATOSA-N Glu-Glu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CCC(O)=O MUSGDMDGNGXULI-DCAQKATOSA-N 0.000 claims 1
- QJCKNLPMTPXXEM-AUTRQRHGSA-N Glu-Glu-Val Chemical compound CC(C)[C@@H](C(O)=O)NC(=O)[C@H](CCC(O)=O)NC(=O)[C@@H](N)CCC(O)=O QJCKNLPMTPXXEM-AUTRQRHGSA-N 0.000 claims 1
- QNJNPKSWAHPYGI-JYJNAYRXSA-N Glu-Phe-Leu Chemical compound OC(=O)CC[C@H](N)C(=O)N[C@H](C(=O)N[C@@H](CC(C)C)C(O)=O)CC1=CC=CC=C1 QNJNPKSWAHPYGI-JYJNAYRXSA-N 0.000 claims 1
- HZISRJBYZAODRV-XQXXSGGOSA-N Glu-Thr-Ala Chemical compound [H]N[C@@H](CCC(O)=O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](C)C(O)=O HZISRJBYZAODRV-XQXXSGGOSA-N 0.000 claims 1
- FGPLUIQCSKGLTI-WDSKDSINSA-N Gly-Ser-Glu Chemical compound NCC(=O)N[C@@H](CO)C(=O)N[C@H](C(O)=O)CCC(O)=O FGPLUIQCSKGLTI-WDSKDSINSA-N 0.000 claims 1
- UROVZOUMHNXPLZ-AVGNSLFASA-N His-Leu-Gln Chemical compound NC(=O)CC[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC1=CN=CN1 UROVZOUMHNXPLZ-AVGNSLFASA-N 0.000 claims 1
- YAALVYQFVJNXIV-KKUMJFAQSA-N His-Leu-Leu Chemical compound CC(C)C[C@@H](C(O)=O)NC(=O)[C@H](CC(C)C)NC(=O)[C@@H](N)CC1=CN=CN1 YAALVYQFVJNXIV-KKUMJFAQSA-N 0.000 claims 1
- UFHFLCQGNIYNRP-UHFFFAOYSA-N Hydrogen Chemical compound [H][H] UFHFLCQGNIYNRP-UHFFFAOYSA-N 0.000 claims 1
- QIHJTGSVGIPHIW-QSFUFRPTSA-N Ile-Asn-Val Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CC(=O)N)C(=O)N[C@@H](C(C)C)C(=O)O)N QIHJTGSVGIPHIW-QSFUFRPTSA-N 0.000 claims 1
- JODPUDMBQBIWCK-GHCJXIJMSA-N Ile-Ser-Asn Chemical compound [H]N[C@@H]([C@@H](C)CC)C(=O)N[C@@H](CO)C(=O)N[C@@H](CC(N)=O)C(O)=O JODPUDMBQBIWCK-GHCJXIJMSA-N 0.000 claims 1
- RQJUKVXWAKJDBW-SVSWQMSJSA-N Ile-Ser-Thr Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](CO)C(=O)N[C@@H]([C@@H](C)O)C(=O)O)N RQJUKVXWAKJDBW-SVSWQMSJSA-N 0.000 claims 1
- WXLYNEHOGRYNFU-URLPEUOOSA-N Ile-Thr-Phe Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)N WXLYNEHOGRYNFU-URLPEUOOSA-N 0.000 claims 1
- UYODHPPSCXBNCS-XUXIUFHCSA-N Ile-Val-Leu Chemical compound CC[C@H](C)[C@H](N)C(=O)N[C@@H](C(C)C)C(=O)N[C@H](C(O)=O)CC(C)C UYODHPPSCXBNCS-XUXIUFHCSA-N 0.000 claims 1
- IBMVEYRWAWIOTN-UHFFFAOYSA-N L-Leucyl-L-Arginyl-L-Proline Natural products CC(C)CC(N)C(=O)NC(CCCN=C(N)N)C(=O)N1CCCC1C(O)=O IBMVEYRWAWIOTN-UHFFFAOYSA-N 0.000 claims 1
- FADYJNXDPBKVCA-UHFFFAOYSA-N L-Phenylalanyl-L-lysin Natural products NCCCCC(C(O)=O)NC(=O)C(N)CC1=CC=CC=C1 FADYJNXDPBKVCA-UHFFFAOYSA-N 0.000 claims 1
- IBMVEYRWAWIOTN-RWMBFGLXSA-N Leu-Arg-Pro Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CCCN=C(N)N)C(=O)N1CCC[C@@H]1C(O)=O IBMVEYRWAWIOTN-RWMBFGLXSA-N 0.000 claims 1
- OIARJGNVARWKFP-YUMQZZPRSA-N Leu-Asn-Gly Chemical compound [H]N[C@@H](CC(C)C)C(=O)N[C@@H](CC(N)=O)C(=O)NCC(O)=O OIARJGNVARWKFP-YUMQZZPRSA-N 0.000 claims 1
- DLCOFDAHNMMQPP-SRVKXCTJSA-N Leu-Asp-Leu Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H](CC(O)=O)C(=O)N[C@@H](CC(C)C)C(O)=O DLCOFDAHNMMQPP-SRVKXCTJSA-N 0.000 claims 1
- ODRREERHVHMIPT-OEAJRASXSA-N Leu-Thr-Phe Chemical compound CC(C)C[C@H](N)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@H](C(O)=O)CC1=CC=CC=C1 ODRREERHVHMIPT-OEAJRASXSA-N 0.000 claims 1
- KNKHAVVBVXKOGX-JXUBOQSCSA-N Lys-Ala-Thr Chemical compound [H]N[C@@H](CCCCN)C(=O)N[C@@H](C)C(=O)N[C@@H]([C@@H](C)O)C(O)=O KNKHAVVBVXKOGX-JXUBOQSCSA-N 0.000 claims 1
- HYSVGEAWTGPMOA-IHRRRGAJSA-N Lys-Pro-Leu Chemical compound [H]N[C@@H](CCCCN)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CC(C)C)C(O)=O HYSVGEAWTGPMOA-IHRRRGAJSA-N 0.000 claims 1
- CNUPMMXDISGXMU-CIUDSAMLSA-N Met-Cys-Glu Chemical compound [H]N[C@@H](CCSC)C(=O)N[C@@H](CS)C(=O)N[C@@H](CCC(O)=O)C(O)=O CNUPMMXDISGXMU-CIUDSAMLSA-N 0.000 claims 1
- WXXNVZMWHOLNRJ-AVGNSLFASA-N Met-Pro-Lys Chemical compound CSCC[C@H](N)C(=O)N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(O)=O WXXNVZMWHOLNRJ-AVGNSLFASA-N 0.000 claims 1
- RMODQFBNDDENCP-IHRRRGAJSA-N Pro-Lys-Leu Chemical compound [H]N1CCC[C@H]1C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(C)C)C(O)=O RMODQFBNDDENCP-IHRRRGAJSA-N 0.000 claims 1
- XQJCEKXQUJQNNK-ZLUOBGJFSA-N Ser-Ser-Ser Chemical compound OC[C@H](N)C(=O)N[C@@H](CO)C(=O)N[C@@H](CO)C(O)=O XQJCEKXQUJQNNK-ZLUOBGJFSA-N 0.000 claims 1
- XVNZSJIKGJLQLH-RCWTZXSCSA-N Thr-Arg-Met Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCCN=C(N)N)C(=O)N[C@@H](CCSC)C(=O)O)N)O XVNZSJIKGJLQLH-RCWTZXSCSA-N 0.000 claims 1
- RKDFEMGVMMYYNG-WDCWCFNPSA-N Thr-Gln-Leu Chemical compound [H]N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCC(N)=O)C(=O)N[C@@H](CC(C)C)C(O)=O RKDFEMGVMMYYNG-WDCWCFNPSA-N 0.000 claims 1
- XYFISNXATOERFZ-OSUNSFLBSA-N Thr-Ile-Val Chemical compound CC[C@H](C)[C@@H](C(=O)N[C@@H](C(C)C)C(=O)O)NC(=O)[C@H]([C@@H](C)O)N XYFISNXATOERFZ-OSUNSFLBSA-N 0.000 claims 1
- MGJLBZFUXUGMML-VOAKCMCISA-N Thr-Lys-Lys Chemical compound C[C@H]([C@@H](C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCCN)C(=O)O)N)O MGJLBZFUXUGMML-VOAKCMCISA-N 0.000 claims 1
- QJIODPFLAASXJC-JHYOHUSXSA-N Thr-Thr-Phe Chemical compound C[C@H]([C@@H](C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CC1=CC=CC=C1)C(=O)O)N)O QJIODPFLAASXJC-JHYOHUSXSA-N 0.000 claims 1
- BURPTJBFWIOHEY-UWJYBYFXSA-N Tyr-Ala-Asp Chemical compound OC(=O)C[C@@H](C(O)=O)NC(=O)[C@H](C)NC(=O)[C@@H](N)CC1=CC=C(O)C=C1 BURPTJBFWIOHEY-UWJYBYFXSA-N 0.000 claims 1
- GITNQBVCEQBDQC-KKUMJFAQSA-N Tyr-Lys-Asn Chemical compound [H]N[C@@H](CC1=CC=C(O)C=C1)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CC(N)=O)C(O)=O GITNQBVCEQBDQC-KKUMJFAQSA-N 0.000 claims 1
- 108010044940 alanylglutamine Proteins 0.000 claims 1
- KOSRFJWDECSPRO-UHFFFAOYSA-N alpha-L-glutamyl-L-glutamic acid Natural products OC(=O)CCC(N)C(=O)NC(CCC(O)=O)C(O)=O KOSRFJWDECSPRO-UHFFFAOYSA-N 0.000 claims 1
- 150000001413 amino acids Chemical group 0.000 claims 1
- 108010077245 asparaginyl-proline Proteins 0.000 claims 1
- 108010038633 aspartylglutamate Proteins 0.000 claims 1
- 238000004440 column chromatography Methods 0.000 claims 1
- 239000003398 denaturant Substances 0.000 claims 1
- 239000003085 diluting agent Substances 0.000 claims 1
- 239000003937 drug carrier Substances 0.000 claims 1
- 239000003480 eluent Substances 0.000 claims 1
- 108010055341 glutamyl-glutamic acid Proteins 0.000 claims 1
- 150000002357 guanidines Chemical class 0.000 claims 1
- 229910052739 hydrogen Inorganic materials 0.000 claims 1
- 239000001257 hydrogen Substances 0.000 claims 1
- 238000002347 injection Methods 0.000 claims 1
- 239000007924 injection Substances 0.000 claims 1
- 108010090333 leucyl-lysyl-proline Proteins 0.000 claims 1
- 238000004811 liquid chromatography Methods 0.000 claims 1
- 108010054155 lysyllysine Proteins 0.000 claims 1
- 238000004519 manufacturing process Methods 0.000 claims 1
- 239000000203 mixture Substances 0.000 claims 1
- 239000002773 nucleotide Substances 0.000 claims 1
- 125000003729 nucleotide group Chemical group 0.000 claims 1
- 239000008194 pharmaceutical composition Substances 0.000 claims 1
- 239000000546 pharmaceutical excipient Substances 0.000 claims 1
- 238000000746 purification Methods 0.000 claims 1
- 239000012266 salt solution Substances 0.000 claims 1
- 239000000243 solution Substances 0.000 claims 1
- 210000004027 cell Anatomy 0.000 description 2
- 239000013612 plasmid Substances 0.000 description 2
- IQFYYKKMVGJFEH-XLPZGREQSA-N Thymidine Chemical class O=C1NC(=O)C(C)=CN1[C@@H]1O[C@H](CO)[C@@H](O)C1 IQFYYKKMVGJFEH-XLPZGREQSA-N 0.000 description 1
- 102000004142 Trypsin Human genes 0.000 description 1
- 108090000631 Trypsin Proteins 0.000 description 1
- 125000003275 alpha amino acid group Chemical group 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 239000013613 expression plasmid Substances 0.000 description 1
- 238000001502 gel electrophoresis Methods 0.000 description 1
- 210000005260 human cell Anatomy 0.000 description 1
- 125000004435 hydrogen atom Chemical group [H]* 0.000 description 1
- 230000007774 longterm Effects 0.000 description 1
- 229920002401 polyacrylamide Polymers 0.000 description 1
- 239000012588 trypsin Substances 0.000 description 1
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- 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
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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
- C07K14/435—Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
- C07K14/52—Cytokines; Lymphokines; Interferons
- C07K14/54—Interleukins [IL]
- C07K14/55—IL-2
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P37/00—Drugs for immunological or allergic disorders
- A61P37/02—Immunomodulators
- A61P37/04—Immunostimulants
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- 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
- C12N15/00—Mutation or genetic engineering; DNA or RNA concerning genetic engineering, vectors, e.g. plasmids, or their isolation, preparation or purification; Use of hosts therefor
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- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
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- Organic Chemistry (AREA)
- Genetics & Genomics (AREA)
- Engineering & Computer Science (AREA)
- General Health & Medical Sciences (AREA)
- Zoology (AREA)
- Medicinal Chemistry (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Molecular Biology (AREA)
- Wood Science & Technology (AREA)
- Biochemistry (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Toxicology (AREA)
- Gastroenterology & Hepatology (AREA)
- Pharmacology & Pharmacy (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Public Health (AREA)
- Animal Behavior & Ethology (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Veterinary Medicine (AREA)
- Physics & Mathematics (AREA)
- Plant Pathology (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Abstract
내용 없음
Description
본 내용은 요부공개 건이므로 전문내용을 수록하지 않았음
제1도 및 제2도는 각각 참고예 1(ⅶ)에서 수득된 플라스미드 pILOT135-8의 제한효소 지도 (는 단일팹티드를 코우딩하는 부분이고,는 IL-2를 코우딩하는 부분이다). 및 상기 플라스미드이 1차 구조(염기서열)를 나타낸다.
제3도는 본 발명에 따른 비글리코실화 인체 IL-2단백질의 아미노산 서열을 나타낸다. 여기서 X는 Met 또는 수소원자이다.
제4도는 참고예 2에 기재된 형질 발현 플라스미드 pTF4의 형성도식을 나타낸다.
제5도는 실시예 1(ⅴ)(1) 및 (2)에서 수행된 SDS-폴리아크릴아미드 평판 겔 전기 영동의 결과를 나타낸다.
제6도는 실시예 1(ⅴ)(6)에 기재된 트립신 분해 팹티드 지도를 나타낸다.
제7도 및 제8도는 각각 실시예 1(ⅴ)(7)에 기재된 NKC3 세포주 및 인체 세포주에 의한 3중 수소화 티미딘의 흡수에 대한 본 발명에 따른 인체 IL-2 단백질의 효과를 나타낸다.
제9도는 실시예 1(ⅴ)(7)에서 수행된 NKC3 세포주의 장기간 계대 배양결과를 나타낸다.
Claims (11)
- 인체 인토로이킨-2를 코우딩한 염기서열을 갖는 DNA를 운반하는 형질 전환체를 성장시켜 배양브로스에 인체 인터로이킨-2를 생성 및 축적시키고, 수득된 인체 인터로이킨-2-함유액체를 소수성 컬럼크로마토그래피에 의해 정제함을 특징으로 하는, 104U/㎎이상의 비활성을 갖는 실제로 순수한 비글리코실화 인체 인터로이킨-2단백질의 제조방법.
- 제1항에 있어서, 단백질이 하기 일반식의 아미노산 서열을 갖는 방법.X-Ala Pro Thr Ser Ser Ser Thr Lys Lys Thr Gln Leu Gln Leu Glu His Leu Leu Leu Asp Leu Gln Met Ile Leu Asn Gly Ile Asn Ans Tyr Lys Asn Pro Lys Leu Thr Arg Met Leu Thr Phe Lys Phe Tyr Met Pro Lys Lys Ala Thr Glu Leu Lys His Leu Gln Cys Leu Glu Glu Glu Leu Lys Pro Leu Glu Glu Val Lnu Asn Leu Ala Gln Ser Lys Asn Phe His Leu Arg Pro Arg Asp Leu Ile Ser Asn Ile Asn Val Ile Val Leu Glu Leu Lys Gly Ser Glu Thr Thr Phe Met Cys Glu Tyr Ala Asp Glu Thr Ala Thr Ile Val Glu Phe Leu Asn Arg Trp Ile Thr Phe Cys Gln Ser Ile Ile Ser Thr Leu Thr(식중 X는 Met 또는 수소이다.)
- 제1항에 있어서, 단백질이 동결건조된 형태인 방법.
- 제1항에 있어서, 소수성컬럼 크로마토그래피가 역상컬럼을 사용한 고수율액체 크로마토그래피인 방법.
- 제4항에 있어서, 크로마토그래피 pH 1.5∼8의 용리액을 사용함으로써 수행되는 방법.
- 제4항에 있어서, 크로마토그래피가 0.1∼100㎖/분의 유속으로 수행되는 방법.
- 제1항에 있어서, 인체 인터로이킨-2를 성장된 형질 변형체 세포에 생성 및 축적시키고, 이인체 인터로이킨-2를 세포로부터 추출하여 인체 인터로이킨-2-함유액체를 수득하는 방법.
- 제7항에 있어서, 인체 인터로이킨-2를 단백질 변성제용액으로 추출하는 방법.
- 제8항에 있어서, 인체 인터로이킨-2를 2∼8M 농도의 구아니딘염 용액으로 추출하는 방법.
- 104U/㎎이상의 비활성을 갖는 실제로 순수한 비클리코실화 인체 인터로이킨-2 단백질을 약학적으로 수용할수 있는 담체, 부형제 또는 희석제와 혼합함을 특징으로 하는, 상기 단백질을 함유한 약학적 조성물의 제조방법.
- 제10항에 있어서, 조성물이 주사용 제제인 방법.※ 참고사항 : 최초출원 내용에 의하여 공개하는 것임.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| JP225079/83 | 1983-11-28 | ||
| JP58225079A JPS60115528A (ja) | 1983-11-28 | 1983-11-28 | ヒトインタ―ロイキン―２蛋白質を含有する抗腫瘍用または免疫機能低下疾患治療用組成物 |
| JP225079 | 1983-11-28 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR850003734A true KR850003734A (ko) | 1985-06-26 |
| KR920006879B1 KR920006879B1 (ko) | 1992-08-21 |
Family
ID=16823684
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019840007430A KR920006879B1 (ko) | 1983-11-28 | 1984-11-27 | 고정제 단백질의 제조방법 |
Country Status (16)
| Country | Link |
|---|---|
| US (1) | US5464939A (ko) |
| EP (3) | EP0442538A1 (ko) |
| JP (1) | JPS60115528A (ko) |
| KR (1) | KR920006879B1 (ko) |
| DK (1) | DK164174C (ko) |
| ES (1) | ES8606489A1 (ko) |
| FI (1) | FI81118C (ko) |
| GR (1) | GR81040B (ko) |
| HU (1) | HU200793B (ko) |
| IL (1) | IL73530A0 (ko) |
| MY (1) | MY103892A (ko) |
| NO (1) | NO169021C (ko) |
| NZ (1) | NZ210352A (ko) |
| PT (1) | PT79555B (ko) |
| SG (1) | SG46452A1 (ko) |
| ZA (1) | ZA849221B (ko) |
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| US4925919A (en) * | 1984-04-25 | 1990-05-15 | Roland Mertelsmann | Purified interleukin 2 |
| US4992271A (en) * | 1982-09-23 | 1991-02-12 | Cetus Corporation | Formulation for lipophilic IL-2 proteins |
| US4853332A (en) * | 1982-10-19 | 1989-08-01 | Cetus Corporation | Structural genes, plasmids and transformed cells for producing cysteine depleted muteins of biologically active proteins |
| DK174501B1 (da) * | 1983-12-23 | 2003-04-28 | Hoffmann La Roche | Fremgangsmåde til fremstilling af interleukin-2 |
| US4569790A (en) * | 1984-03-28 | 1986-02-11 | Cetus Corporation | Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions |
| JPS60243021A (ja) * | 1984-03-28 | 1985-12-03 | シタス コ−ポレイシヨン | システイン含有蛋白質の制御された酸化方法 |
| EP0158487B1 (en) * | 1984-04-09 | 1991-08-28 | Takeda Chemical Industries, Ltd. | Stable composition of interleukin-2 |
| US4908434A (en) * | 1984-04-25 | 1990-03-13 | Sloan-Kettering Institute For Cancer Research | Process for preparing purified interleukin-2 |
| US4908433A (en) * | 1984-04-25 | 1990-03-13 | Sloan-Kettering Institute For Cancer Research | Uses of interleukin-2 |
| IL76360A0 (en) | 1984-09-26 | 1986-01-31 | Takeda Chemical Industries Ltd | Mutual separation of proteins |
| WO1986002068A1 (en) * | 1984-09-26 | 1986-04-10 | Takeda Chemical Industries, Ltd. | Mutual separation of proteins |
| JPH0646957B2 (ja) * | 1985-03-11 | 1994-06-22 | 武田薬品工業株式会社 | インタ−ロイキン−２の製造方法 |
| WO1986007093A1 (en) * | 1985-05-29 | 1986-12-04 | The Green Cross Corporation | Process for preparing heterogenic protein |
| US4748234A (en) * | 1985-06-26 | 1988-05-31 | Cetus Corporation | Process for recovering refractile bodies containing heterologous proteins from microbial hosts |
| DE3581412D1 (de) * | 1985-07-16 | 1991-02-21 | Green Cross Corp | Verfahren zur herstellung von heteroproteinen. |
| DE3526096A1 (de) * | 1985-07-22 | 1987-01-22 | Basf Ag | Verfahren zur reinigung von htnf |
| CN86104525A (zh) * | 1985-07-31 | 1987-02-25 | 武田药品工业株式会社 | 人类白细胞介素-2的分析方法和试剂 |
| DK585886A (da) * | 1985-12-24 | 1987-06-25 | Takeda Chemical Industries Ltd | Immunstimulerende middel og anvendelse deraf |
| US4933433A (en) * | 1986-01-31 | 1990-06-12 | E. I. Du Pont De Nemours And Company | Recombinant interleukin-2 composition and process for making it |
| JPH0655153B2 (ja) * | 1986-02-26 | 1994-07-27 | 武田薬品工業株式会社 | ヒトインターロイキン―２結晶の製造法 |
| CA1339757C (en) * | 1987-04-16 | 1998-03-17 | Robert F. Halenbeck | Production of purified biologically active, bacterially produced recombinant human csf-1 |
| US4929700A (en) * | 1987-04-16 | 1990-05-29 | Cetus Corporation | Production of purified, biologically active, bacterially produced recombinant human CSF-1 |
| US4961969A (en) * | 1987-05-11 | 1990-10-09 | Cetus Corporation | Process for recovering microbially produced interferon-β |
| US4931543A (en) * | 1987-05-11 | 1990-06-05 | Cetus Corporation | Process for recovering microbially produced interleukin-2 |
| US5149788A (en) * | 1987-05-19 | 1992-09-22 | Hoffmann-La Roche, Inc. | Purification of chimeric proteins containing an IL-2 moiety by receptor-affinity chromatography |
| US5162503A (en) * | 1987-05-19 | 1992-11-10 | Hoffmann-La Roche, Inc. | Purification of interleukin-2 by receptor-affinity chromatography |
| FR2635527B1 (fr) * | 1988-07-28 | 1992-06-12 | Roussel Uclaf | Il2 humaine recombinante non glycosylee sous forme reduite, son procede d'obtention et son application comme medicament |
| US5250296A (en) * | 1990-11-29 | 1993-10-05 | Takeda Chemical Industries, Ltd. | Immunostimulant agent containing interleukin-2 and 5'-deoxy-5-fluorouridine |
| US5416071A (en) * | 1991-03-12 | 1995-05-16 | Takeda Chemical Industries, Ltd. | Water-soluble composition for sustained-release containing epo and hyaluronic acid |
| CA2471363C (en) | 2001-12-21 | 2014-02-11 | Human Genome Sciences, Inc. | Albumin fusion proteins |
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| WO2012065086A1 (en) * | 2010-11-12 | 2012-05-18 | Nektar Therapeutics | Conjugates of an il-2 moiety and a polymer |
| EP3204119B1 (en) | 2014-10-09 | 2021-06-09 | Dana-Farber Cancer Institute, Inc. | Multiple-variable il-2 dose regimen for treating immune disorders |
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| JPS58116498A (ja) * | 1981-12-28 | 1983-07-11 | Takeda Chem Ind Ltd | Ｉｌ‐２をコードする新規伝令ｒｎａの製造法 |
| JPH0751511B2 (ja) * | 1982-03-15 | 1995-06-05 | 味の素株式会社 | インターロイキン２を含有してなる癌治療剤 |
| CA1210714A (en) * | 1982-03-23 | 1986-09-02 | Alan Sloma | .alpha.-INTERFERON GX-1 |
| US4738927A (en) * | 1982-03-31 | 1988-04-19 | Ajinomoto Co. Inc. | Gene coded for interleukin-2 polypeptide, recombinant DNA carrying the said gene, a living cell line possessing the recombinant DNA, and method for producing interleukin-2 using the said cell |
| JPS58201979A (ja) * | 1982-05-18 | 1983-11-25 | Japan Found Cancer | ヒトインタ−ロイキン２遺伝子が組込まれているエシエリヒア・コリおよびその育種方法 |
| CA1341562C (en) * | 1982-03-31 | 2007-11-27 | Tadatsugu Taniguchi | Gene coded for interleukin-2 polypeptide, recombinant dna carrying the said gene, a living cell line possessing the recombinant dna, and method for producing interleukin-2 using the said cell |
| JPS58168492A (ja) * | 1982-03-31 | 1983-10-04 | Nippon Kokan Kk <Nkk> | パイプ切断機 |
| DE3378128D1 (en) * | 1982-04-20 | 1988-11-03 | Sloan Kettering Inst Cancer | Purification of interleukin 2 |
| JPS58198293A (ja) * | 1982-05-12 | 1983-11-18 | Shionogi & Co Ltd | インタ−ロイキン等免疫調節因子の製造方法 |
| NL8203321A (nl) * | 1982-08-25 | 1984-03-16 | Philips Nv | Kleurenbeeldbuis. |
| US4490289A (en) * | 1982-09-16 | 1984-12-25 | Hoffmann-La Roche Inc. | Homogeneous human interleukin 2 |
| AU579089B2 (en) * | 1983-02-08 | 1988-11-17 | Biogen, Inc. | Human interleukin-2-like polypeptides |
| IL71275A0 (en) * | 1983-03-21 | 1984-06-29 | Sparamedica Ag | Human interleukin-2-and its preparation |
| US4518584A (en) * | 1983-04-15 | 1985-05-21 | Cetus Corporation | Human recombinant interleukin-2 muteins |
| JPS61500586A (ja) * | 1983-11-14 | 1986-04-03 | チロン コ−ポレイシヨン | インタ−ロイキン−２産生のための方法及び組成物 |
| DK174501B1 (da) * | 1983-12-23 | 2003-04-28 | Hoffmann La Roche | Fremgangsmåde til fremstilling af interleukin-2 |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| US4569790A (en) * | 1984-03-28 | 1986-02-11 | Cetus Corporation | Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions |
| JP2608730B2 (ja) * | 1987-08-10 | 1997-05-14 | 株式会社リコー | 感熱記録材料 |
-
1983
- 1983-11-28 JP JP58225079A patent/JPS60115528A/ja active Granted
-
1984
- 1984-11-16 IL IL73530A patent/IL73530A0/xx unknown
- 1984-11-23 EP EP19910105904 patent/EP0442538A1/en not_active Withdrawn
- 1984-11-23 EP EP84308153A patent/EP0145390A3/en not_active Ceased
- 1984-11-23 SG SG1996004789A patent/SG46452A1/en unknown
- 1984-11-23 EP EP96201538A patent/EP0751220A1/en not_active Ceased
- 1984-11-26 ZA ZA849221A patent/ZA849221B/xx unknown
- 1984-11-26 GR GR81040A patent/GR81040B/el unknown
- 1984-11-27 ES ES537994A patent/ES8606489A1/es not_active Expired
- 1984-11-27 NO NO844710A patent/NO169021C/no unknown
- 1984-11-27 HU HU844383A patent/HU200793B/hu not_active IP Right Cessation
- 1984-11-27 KR KR1019840007430A patent/KR920006879B1/ko not_active IP Right Cessation
- 1984-11-27 DK DK560784A patent/DK164174C/da not_active IP Right Cessation
- 1984-11-27 NZ NZ210352A patent/NZ210352A/xx unknown
- 1984-11-27 PT PT79555A patent/PT79555B/pt not_active IP Right Cessation
- 1984-11-28 FI FI844678A patent/FI81118C/fi not_active IP Right Cessation
-
1987
- 1987-09-28 MY MYPI87002002A patent/MY103892A/en unknown
-
1992
- 1992-09-09 US US07/942,358 patent/US5464939A/en not_active Expired - Lifetime
Also Published As
| Publication number | Publication date |
|---|---|
| ZA849221B (en) | 1986-07-30 |
| JPS60115528A (ja) | 1985-06-22 |
| AU3575684A (en) | 1985-06-06 |
| ES537994A0 (es) | 1986-04-01 |
| KR920006879B1 (ko) | 1992-08-21 |
| DK560784A (da) | 1985-05-29 |
| FI81118B (fi) | 1990-05-31 |
| DK164174C (da) | 1992-10-05 |
| US5464939A (en) | 1995-11-07 |
| NO169021B (no) | 1992-01-20 |
| MY103892A (en) | 1993-10-30 |
| HUT36186A (en) | 1985-08-28 |
| NZ210352A (en) | 1988-11-29 |
| FI844678L (fi) | 1985-05-29 |
| DK164174B (da) | 1992-05-18 |
| AU592527B2 (en) | 1990-01-18 |
| FI844678A0 (fi) | 1984-11-28 |
| PT79555B (en) | 1986-12-15 |
| SG46452A1 (en) | 1998-02-20 |
| GR81040B (en) | 1985-03-27 |
| DK560784D0 (da) | 1984-11-27 |
| IL73530A0 (en) | 1985-02-28 |
| NO169021C (no) | 1992-04-29 |
| FI81118C (fi) | 1990-09-10 |
| PT79555A (en) | 1984-12-01 |
| HU200793B (en) | 1990-08-28 |
| EP0145390A3 (en) | 1987-01-21 |
| EP0751220A1 (en) | 1997-01-02 |
| EP0442538A1 (en) | 1991-08-21 |
| JPH0542413B2 (ko) | 1993-06-28 |
| EP0145390A2 (en) | 1985-06-19 |
| NO844710L (no) | 1985-05-29 |
| ES8606489A1 (es) | 1986-04-01 |
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