IE59100B1 - Purified recombinant interleukin-2 and process for recovering and purifying same - Google Patents
Purified recombinant interleukin-2 and process for recovering and purifying sameInfo
- Publication number
- IE59100B1 IE59100B1 IE79985A IE79985A IE59100B1 IE 59100 B1 IE59100 B1 IE 59100B1 IE 79985 A IE79985 A IE 79985A IE 79985 A IE79985 A IE 79985A IE 59100 B1 IE59100 B1 IE 59100B1
- Authority
- IE
- Ireland
- Prior art keywords
- process according
- solution
- agent
- gel filtration
- solubilizing
- Prior art date
Links
- 108010002350 Interleukin-2 Proteins 0.000 title claims abstract description 93
- 238000000034 method Methods 0.000 title claims abstract description 48
- 230000008569 process Effects 0.000 title claims abstract description 24
- 102000000588 Interleukin-2 Human genes 0.000 title claims description 88
- 239000000243 solution Substances 0.000 claims abstract description 29
- 238000000605 extraction Methods 0.000 claims abstract description 22
- 239000002904 solvent Substances 0.000 claims abstract description 21
- 238000004007 reversed phase HPLC Methods 0.000 claims abstract description 20
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims abstract description 18
- 244000005700 microbiome Species 0.000 claims abstract description 18
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- 239000004202 carbamide Substances 0.000 claims abstract description 10
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- 230000003381 solubilizing effect Effects 0.000 claims abstract description 4
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- 238000002523 gelfiltration Methods 0.000 claims description 15
- 239000012071 phase Substances 0.000 claims description 7
- 239000002253 acid Substances 0.000 claims description 4
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 claims description 3
- DBMJMQXJHONAFJ-UHFFFAOYSA-M Sodium laurylsulphate Chemical group [Na+].CCCCCCCCCCCCOS([O-])(=O)=O DBMJMQXJHONAFJ-UHFFFAOYSA-M 0.000 claims description 2
- 230000001376 precipitating effect Effects 0.000 claims description 2
- 238000004811 liquid chromatography Methods 0.000 claims 1
- 229910052708 sodium Inorganic materials 0.000 claims 1
- 239000011734 sodium Substances 0.000 claims 1
- 108090000623 proteins and genes Proteins 0.000 abstract description 32
- 102000004169 proteins and genes Human genes 0.000 abstract description 32
- BTANRVKWQNVYAZ-UHFFFAOYSA-N butan-2-ol Chemical compound CCC(C)O BTANRVKWQNVYAZ-UHFFFAOYSA-N 0.000 abstract description 10
- MSXVEPNJUHWQHW-UHFFFAOYSA-N 2-methylbutan-2-ol Chemical compound CCC(C)(C)O MSXVEPNJUHWQHW-UHFFFAOYSA-N 0.000 abstract description 9
- 230000000813 microbial effect Effects 0.000 abstract 1
- 230000001590 oxidative effect Effects 0.000 abstract 1
- 235000018102 proteins Nutrition 0.000 description 31
- LRHPLDYGYMQRHN-UHFFFAOYSA-N N-Butanol Chemical compound CCCCO LRHPLDYGYMQRHN-UHFFFAOYSA-N 0.000 description 18
- 239000000047 product Substances 0.000 description 17
- WEVYAHXRMPXWCK-UHFFFAOYSA-N Acetonitrile Chemical compound CC#N WEVYAHXRMPXWCK-UHFFFAOYSA-N 0.000 description 12
- 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 12
- 239000000872 buffer Substances 0.000 description 11
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- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 9
- 241000588724 Escherichia coli Species 0.000 description 8
- 101001002657 Homo sapiens Interleukin-2 Proteins 0.000 description 8
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- 125000000151 cysteine group Chemical group N[C@@H](CS)C(=O)* 0.000 description 7
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- 238000005063 solubilization Methods 0.000 description 7
- 230000007928 solubilization Effects 0.000 description 7
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 7
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- WQZGKKKJIJFFOK-GASJEMHNSA-N Glucose Natural products OC[C@H]1OC(O)[C@H](O)[C@@H](O)[C@@H]1O WQZGKKKJIJFFOK-GASJEMHNSA-N 0.000 description 3
- QIVBCDIJIAJPQS-VIFPVBQESA-N L-tryptophane Chemical compound C1=CC=C2C(C[C@H](N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-VIFPVBQESA-N 0.000 description 3
- MTCFGRXMJLQNBG-UHFFFAOYSA-N Serine Natural products OCC(N)C(O)=O MTCFGRXMJLQNBG-UHFFFAOYSA-N 0.000 description 3
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- LEVWYRKDKASIDU-QWWZWVQMSA-N D-cystine Chemical compound OC(=O)[C@H](N)CSSC[C@@H](N)C(O)=O LEVWYRKDKASIDU-QWWZWVQMSA-N 0.000 description 2
- 230000005526 G1 to G0 transition Effects 0.000 description 2
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- 229960004799 tryptophan Drugs 0.000 description 2
- 238000000108 ultra-filtration Methods 0.000 description 2
- BMYCCWYAFNPAQC-UHFFFAOYSA-N 2-[dodecyl(methyl)azaniumyl]acetate Chemical compound CCCCCCCCCCCCN(C)CC(O)=O BMYCCWYAFNPAQC-UHFFFAOYSA-N 0.000 description 1
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- KRKNYBCHXYNGOX-UHFFFAOYSA-K Citrate Chemical compound [O-]C(=O)CC(O)(CC([O-])=O)C([O-])=O KRKNYBCHXYNGOX-UHFFFAOYSA-K 0.000 description 1
- 241001646716 Escherichia coli K-12 Species 0.000 description 1
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- 102100026720 Interferon beta Human genes 0.000 description 1
- 108090000467 Interferon-beta Proteins 0.000 description 1
- QNAYBMKLOCPYGJ-REOHCLBHSA-N L-alanine Chemical compound C[C@H](N)C(O)=O QNAYBMKLOCPYGJ-REOHCLBHSA-N 0.000 description 1
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- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
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- 239000003226 mitogen Substances 0.000 description 1
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- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 235000016709 nutrition Nutrition 0.000 description 1
- 150000007524 organic acids Chemical class 0.000 description 1
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- 238000007911 parenteral administration Methods 0.000 description 1
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- 239000008363 phosphate buffer Substances 0.000 description 1
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- 150000003522 tetracyclines Chemical class 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
- 230000009385 viral infection Effects 0.000 description 1
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- NWONKYPBYAMBJT-UHFFFAOYSA-L zinc sulfate Chemical compound [Zn+2].[O-]S([O-])(=O)=O NWONKYPBYAMBJT-UHFFFAOYSA-L 0.000 description 1
Classifications
-
- 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
-
- 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
- C07K1/1133—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 redox-reactions involving cystein/cystin side chains
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P35/00—Antineoplastic agents
-
- 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
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Life Sciences & Earth Sciences (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Biochemistry (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Molecular Biology (AREA)
- Biophysics (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Zoology (AREA)
- General Chemical & Material Sciences (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Gastroenterology & Hepatology (AREA)
- Toxicology (AREA)
- Biotechnology (AREA)
- General Engineering & Computer Science (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Analytical Chemistry (AREA)
- Biomedical Technology (AREA)
- Animal Behavior & Ethology (AREA)
- Physics & Mathematics (AREA)
- Veterinary Medicine (AREA)
- Public Health (AREA)
- Plant Pathology (AREA)
- Pharmacology & Pharmacy (AREA)
- Microbiology (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Peptides Or Proteins (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
- Micro-Organisms Or Cultivation Processes Thereof (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US06/594,223 US4569790A (en) | 1984-03-28 | 1984-03-28 | Process for recovering microbially produced interleukin-2 and purified recombinant interleukin-2 compositions |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| IE850799L IE850799L (en) | 1985-09-28 |
| IE59100B1 true IE59100B1 (en) | 1994-01-12 |
Family
ID=24378044
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| IE79985A IE59100B1 (en) | 1984-03-28 | 1985-03-28 | Purified recombinant interleukin-2 and process for recovering and purifying same |
Country Status (20)
| Country | Link |
|---|---|
| US (3) | US4569790A (OSRAM) |
| EP (2) | EP0470586B1 (OSRAM) |
| JP (2) | JP2599903B2 (OSRAM) |
| KR (1) | KR850007083A (OSRAM) |
| AT (1) | ATE81674T1 (OSRAM) |
| AU (1) | AU592751B2 (OSRAM) |
| CA (1) | CA1341083C (OSRAM) |
| DE (2) | DE3586762T2 (OSRAM) |
| DK (1) | DK166324C (OSRAM) |
| ES (1) | ES8609362A1 (OSRAM) |
| FI (1) | FI94960C (OSRAM) |
| GR (1) | GR850741B (OSRAM) |
| IE (1) | IE59100B1 (OSRAM) |
| IL (1) | IL74733A (OSRAM) |
| IN (1) | IN162903B (OSRAM) |
| NO (1) | NO851235L (OSRAM) |
| NZ (1) | NZ211569A (OSRAM) |
| PH (1) | PH21012A (OSRAM) |
| PT (1) | PT80172B (OSRAM) |
| ZA (1) | ZA852347B (OSRAM) |
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- 1985-03-27 DE DE3588189T patent/DE3588189T2/de not_active Expired - Lifetime
- 1985-03-28 JP JP60062195A patent/JP2599903B2/ja not_active Expired - Lifetime
- 1985-03-28 ZA ZA852347A patent/ZA852347B/xx unknown
- 1985-03-28 KR KR1019850002078A patent/KR850007083A/ko not_active Ceased
- 1985-03-28 AU AU40467/85A patent/AU592751B2/en not_active Expired
- 1985-03-28 IE IE79985A patent/IE59100B1/en not_active IP Right Cessation
-
1992
- 1992-05-06 US US07/879,753 patent/US5419899A/en not_active Expired - Lifetime
-
1995
- 1995-04-25 US US08/428,895 patent/US5614185A/en not_active Expired - Lifetime
-
1996
- 1996-05-15 JP JP8143485A patent/JP2648587B2/ja not_active Expired - Lifetime
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| MK9A | Patent expired |