NL8700397A - Zuivering van recombinant humaan-interleukine-1. - Google Patents
Zuivering van recombinant humaan-interleukine-1. Download PDFInfo
- Publication number
- NL8700397A NL8700397A NL8700397A NL8700397A NL8700397A NL 8700397 A NL8700397 A NL 8700397A NL 8700397 A NL8700397 A NL 8700397A NL 8700397 A NL8700397 A NL 8700397A NL 8700397 A NL8700397 A NL 8700397A
- Authority
- NL
- Netherlands
- Prior art keywords
- human interleukin
- gradient
- tris
- interleukin
- buffered
- Prior art date
Links
- 238000000746 purification Methods 0.000 title description 9
- 108010002352 Interleukin-1 Proteins 0.000 claims description 28
- 102000000589 Interleukin-1 Human genes 0.000 claims description 27
- 238000000034 method Methods 0.000 claims description 25
- 108090000623 proteins and genes Proteins 0.000 claims description 23
- 102000004169 proteins and genes Human genes 0.000 claims description 20
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 claims description 18
- 210000004027 cell Anatomy 0.000 claims description 17
- 239000007983 Tris buffer Substances 0.000 claims description 12
- 230000000694 effects Effects 0.000 claims description 11
- 239000012506 Sephacryl® Substances 0.000 claims description 9
- 210000000172 cytosol Anatomy 0.000 claims description 9
- 239000011780 sodium chloride Substances 0.000 claims description 9
- GUBGYTABKSRVRQ-WFVLMXAXSA-N DEAE-cellulose Chemical compound OC1C(O)C(O)C(CO)O[C@H]1O[C@@H]1C(CO)OC(O)C(O)C1O GUBGYTABKSRVRQ-WFVLMXAXSA-N 0.000 claims description 6
- 239000007975 buffered saline Substances 0.000 claims description 6
- 230000001965 increasing effect Effects 0.000 claims description 6
- 239000000243 solution Substances 0.000 claims description 5
- 201000010099 disease Diseases 0.000 claims description 4
- 208000037265 diseases, disorders, signs and symptoms Diseases 0.000 claims description 4
- 150000003839 salts Chemical class 0.000 claims description 4
- 238000011282 treatment Methods 0.000 claims description 4
- 125000003275 alpha amino acid group Chemical group 0.000 claims description 3
- 239000000872 buffer Substances 0.000 claims description 3
- 239000008366 buffered solution Substances 0.000 claims description 3
- 238000002523 gelfiltration Methods 0.000 claims description 3
- 238000004255 ion exchange chromatography Methods 0.000 claims description 3
- 239000013604 expression vector Substances 0.000 claims description 2
- 239000000825 pharmaceutical preparation Substances 0.000 claims description 2
- 238000011321 prophylaxis Methods 0.000 claims description 2
- 238000009210 therapy by ultrasound Methods 0.000 claims description 2
- 238000001641 gel filtration chromatography Methods 0.000 claims 1
- 230000001939 inductive effect Effects 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 19
- 239000002158 endotoxin Substances 0.000 description 7
- 238000004587 chromatography analysis Methods 0.000 description 5
- 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 4
- 241000588724 Escherichia coli Species 0.000 description 4
- 238000005119 centrifugation Methods 0.000 description 4
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 4
- 239000006228 supernatant Substances 0.000 description 4
- WEEMDRWIKYCTQM-UHFFFAOYSA-N 2,6-dimethoxybenzenecarbothioamide Chemical compound COC1=CC=CC(OC)=C1C(N)=S WEEMDRWIKYCTQM-UHFFFAOYSA-N 0.000 description 3
- QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 3
- 238000004458 analytical method Methods 0.000 description 3
- 230000004071 biological effect Effects 0.000 description 3
- 238000004440 column chromatography Methods 0.000 description 3
- 239000003550 marker Substances 0.000 description 3
- 229960002385 streptomycin sulfate Drugs 0.000 description 3
- BFSVOASYOCHEOV-UHFFFAOYSA-N 2-diethylaminoethanol Chemical compound CCN(CC)CCO BFSVOASYOCHEOV-UHFFFAOYSA-N 0.000 description 2
- XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 description 2
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 2
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 2
- 235000011130 ammonium sulphate Nutrition 0.000 description 2
- 230000001580 bacterial effect Effects 0.000 description 2
- 239000004202 carbamide Substances 0.000 description 2
- 239000003795 chemical substances by application Substances 0.000 description 2
- 239000000463 material Substances 0.000 description 2
- 102000039446 nucleic acids Human genes 0.000 description 2
- 108020004707 nucleic acids Proteins 0.000 description 2
- 150000007523 nucleic acids Chemical class 0.000 description 2
- 238000002360 preparation method Methods 0.000 description 2
- 239000000047 product Substances 0.000 description 2
- 239000013049 sediment Substances 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- QKNYBSVHEMOAJP-UHFFFAOYSA-N 2-amino-2-(hydroxymethyl)propane-1,3-diol;hydron;chloride Chemical compound Cl.OCC(N)(CO)CO QKNYBSVHEMOAJP-UHFFFAOYSA-N 0.000 description 1
- 241000894006 Bacteria Species 0.000 description 1
- 108091003079 Bovine Serum Albumin Proteins 0.000 description 1
- 102000003846 Carbonic anhydrases Human genes 0.000 description 1
- 108090000209 Carbonic anhydrases Proteins 0.000 description 1
- 208000028399 Critical Illness Diseases 0.000 description 1
- 235000010469 Glycine max Nutrition 0.000 description 1
- 244000068988 Glycine max Species 0.000 description 1
- 241000282412 Homo Species 0.000 description 1
- 102000004407 Lactalbumin Human genes 0.000 description 1
- 108090000942 Lactalbumin Proteins 0.000 description 1
- 102100033468 Lysozyme C Human genes 0.000 description 1
- 241000124008 Mammalia Species 0.000 description 1
- 108010014251 Muramidase Proteins 0.000 description 1
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 1
- 108010058846 Ovalbumin Proteins 0.000 description 1
- 108010065081 Phosphorylase b Proteins 0.000 description 1
- 101710162629 Trypsin inhibitor Proteins 0.000 description 1
- 229940122618 Trypsin inhibitor Drugs 0.000 description 1
- 239000000654 additive Substances 0.000 description 1
- 150000001450 anions Chemical class 0.000 description 1
- 238000003556 assay Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 229940098773 bovine serum albumin Drugs 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 238000001516 cell proliferation assay Methods 0.000 description 1
- 239000006285 cell suspension Substances 0.000 description 1
- 238000003776 cleavage reaction Methods 0.000 description 1
- 238000010367 cloning Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000011109 contamination Methods 0.000 description 1
- 238000002788 crimping Methods 0.000 description 1
- 230000006378 damage Effects 0.000 description 1
- 230000007123 defense Effects 0.000 description 1
- 230000029087 digestion Effects 0.000 description 1
- 239000002552 dosage form Substances 0.000 description 1
- 239000003480 eluent Substances 0.000 description 1
- 230000002708 enhancing effect Effects 0.000 description 1
- 230000007515 enzymatic degradation Effects 0.000 description 1
- 238000005227 gel permeation chromatography Methods 0.000 description 1
- 229960000789 guanidine hydrochloride Drugs 0.000 description 1
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 1
- 230000035876 healing Effects 0.000 description 1
- 230000028993 immune response Effects 0.000 description 1
- 210000000987 immune system Anatomy 0.000 description 1
- 210000003000 inclusion body Anatomy 0.000 description 1
- 230000002452 interceptive effect Effects 0.000 description 1
- 238000007918 intramuscular administration Methods 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 238000004519 manufacturing process Methods 0.000 description 1
- 125000001360 methionine group Chemical group N[C@@H](CCSC)C(=O)* 0.000 description 1
- 230000000813 microbial effect Effects 0.000 description 1
- 230000037230 mobility Effects 0.000 description 1
- 230000001613 neoplastic effect Effects 0.000 description 1
- 229910052757 nitrogen Inorganic materials 0.000 description 1
- 125000004433 nitrogen atom Chemical group N* 0.000 description 1
- 208000015380 nutritional deficiency disease Diseases 0.000 description 1
- 229940092253 ovalbumin Drugs 0.000 description 1
- 238000007911 parenteral administration Methods 0.000 description 1
- 239000006201 parenteral dosage form Substances 0.000 description 1
- 244000052769 pathogen Species 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 230000001737 promoting effect Effects 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 229940124272 protein stabilizer Drugs 0.000 description 1
- 239000013014 purified material Substances 0.000 description 1
- 238000004007 reversed phase HPLC Methods 0.000 description 1
- 230000007017 scission Effects 0.000 description 1
- 230000028327 secretion Effects 0.000 description 1
- 238000000926 separation method Methods 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000003381 stabilizer Substances 0.000 description 1
- 230000004936 stimulating effect Effects 0.000 description 1
- 238000007920 subcutaneous administration Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 230000001960 triggered effect Effects 0.000 description 1
- 239000002753 trypsin inhibitor Substances 0.000 description 1
- 238000002604 ultrasonography Methods 0.000 description 1
- 239000012646 vaccine adjuvant Substances 0.000 description 1
- 229940124931 vaccine adjuvant Drugs 0.000 description 1
- 230000029663 wound healing Effects 0.000 description 1
- 235000021241 α-lactalbumin Nutrition 0.000 description 1
Classifications
-
- 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]
- C07K14/545—IL-1
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P1/00—Drugs for disorders of the alimentary tract or the digestive system
- A61P1/04—Drugs for disorders of the alimentary tract or the digestive system for ulcers, gastritis or reflux esophagitis, e.g. antacids, inhibitors of acid secretion, mucosal protectants
-
- Y—GENERAL TAGGING OF NEW TECHNOLOGICAL DEVELOPMENTS; GENERAL TAGGING OF CROSS-SECTIONAL TECHNOLOGIES SPANNING OVER SEVERAL SECTIONS OF THE IPC; TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10—TECHNICAL SUBJECTS COVERED BY FORMER USPC
- Y10S—TECHNICAL SUBJECTS COVERED BY FORMER USPC CROSS-REFERENCE ART COLLECTIONS [XRACs] AND DIGESTS
- Y10S930/00—Peptide or protein sequence
- Y10S930/01—Peptide or protein sequence
- Y10S930/14—Lymphokine; related peptides
- Y10S930/141—Interleukin
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- General Health & Medical Sciences (AREA)
- Medicinal Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biophysics (AREA)
- Biochemistry (AREA)
- Genetics & Genomics (AREA)
- Gastroenterology & Hepatology (AREA)
- Molecular Biology (AREA)
- Zoology (AREA)
- Toxicology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Engineering & Computer Science (AREA)
- Chemical Kinetics & Catalysis (AREA)
- General Chemical & Material Sciences (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Pharmacology & Pharmacy (AREA)
- Animal Behavior & Ethology (AREA)
- Public Health (AREA)
- Veterinary Medicine (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
Applications Claiming Priority (2)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US83040686 | 1986-02-18 | ||
| US06/830,406 US5831022A (en) | 1986-02-18 | 1986-02-18 | Purification of recombinant human IL-1α |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| NL8700397A true NL8700397A (nl) | 1987-09-16 |
Family
ID=25256938
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| NL8700397A NL8700397A (nl) | 1986-02-18 | 1987-02-17 | Zuivering van recombinant humaan-interleukine-1. |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US5831022A (enExample) |
| JP (1) | JP2590085B2 (enExample) |
| BE (1) | BE1000636A5 (enExample) |
| CH (1) | CH676008A5 (enExample) |
| DE (1) | DE3704868C2 (enExample) |
| DK (1) | DK171419B1 (enExample) |
| FR (1) | FR2595714B1 (enExample) |
| GB (1) | GB2186580B (enExample) |
| IT (1) | IT1202565B (enExample) |
| NL (1) | NL8700397A (enExample) |
Families Citing this family (4)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| ATE92766T1 (de) * | 1987-12-18 | 1993-08-15 | Immunex Corp | Oertliche wundheilmittel, die interleukin-1proteine enthalten. |
| US5120534A (en) * | 1988-07-29 | 1992-06-09 | Otsuka Pharmaceutical Co., Ltd. | IL-1α derivatives and medicament for treating thrombocytopenia |
| IT1226713B (it) * | 1988-08-05 | 1991-02-05 | Eniricerche Spa | Procedimento per la preparazione di interleuchina 1 beta umana ricombinante in forma omogenea. |
| CZ296806B6 (cs) * | 1994-10-24 | 2006-06-14 | Allergan, Inc. | Rozpustný fúzní protein a zpusob výroby rozpustného rekombinantního botulinového toxinu |
Family Cites Families (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4401756A (en) * | 1981-04-14 | 1983-08-30 | Immunex Corporation | Process for preparing human interleukin 2 |
| 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 |
| GR79124B (enExample) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
| FR2550802B1 (fr) * | 1983-08-17 | 1986-04-11 | Inst Nat Sante Rech Med | Procede de production d'interleukine 1 humaine et medicaments correspondants |
| DK174501B1 (da) * | 1983-12-23 | 2003-04-28 | Hoffmann La Roche | Fremgangsmåde til fremstilling af interleukin-2 |
| JPS60149386A (ja) * | 1984-01-17 | 1985-08-06 | Dainippon Pharmaceut Co Ltd | インタ−ロイキン１をコ−ドする伝令リボ核酸及びその調製法 |
| JPS60197629A (ja) * | 1984-03-16 | 1985-10-07 | Chemo Sero Therapeut Res Inst | ＨＢｓ抗原の精製方法 |
| DE3419995A1 (de) * | 1984-05-29 | 1985-12-05 | Hoechst Ag, 6230 Frankfurt | Gentechnologisches verfahren zur herstellung von human-interleukin-2 und mittel zur durchfuehrung dieses verfahrens |
| JPS617296A (ja) * | 1984-06-19 | 1986-01-13 | イミユネツクス、コ−ポレ−シヨン | インタ−ロイキン１の遺伝子の精製、クロ−ニング及び特性づけ |
| CA1341433C (en) * | 1984-06-19 | 2003-06-24 | Douglas P. Cerretti | Purification of interleukin 1 |
| DE3432196A1 (de) * | 1984-09-01 | 1986-03-06 | Boehringer Ingelheim International GmbH, 6507 Ingelheim | Neues mechanisches aufschlussverfahren von bakterienzellen zur isolierung von rekombinant hergestellten peptiden |
| DE3683186D1 (de) * | 1985-04-25 | 1992-02-13 | Hoffmann La Roche | Rekombinantes humaninterleukin-1. |
| US4675387A (en) * | 1985-07-26 | 1987-06-23 | E. I. Du Pont De Nemours And Company | Method for extracting protein with organic acid |
| US5008374A (en) * | 1986-03-14 | 1991-04-16 | Otsuka Pharmaceutical Co., Ltd. | IL-1α derivatives and drugs |
| US4801686A (en) * | 1986-09-04 | 1989-01-31 | Immunex Corporation | Purification of recombinant interleukin-1 |
-
1986
- 1986-02-18 US US06/830,406 patent/US5831022A/en not_active Expired - Lifetime
-
1987
- 1987-01-13 CH CH98/87A patent/CH676008A5/de not_active IP Right Cessation
- 1987-02-12 FR FR878702010A patent/FR2595714B1/fr not_active Expired - Lifetime
- 1987-02-16 DK DK077387A patent/DK171419B1/da not_active IP Right Cessation
- 1987-02-16 DE DE3704868A patent/DE3704868C2/de not_active Expired - Fee Related
- 1987-02-17 GB GB8703663A patent/GB2186580B/en not_active Expired - Lifetime
- 1987-02-17 JP JP62034385A patent/JP2590085B2/ja not_active Expired - Lifetime
- 1987-02-17 NL NL8700397A patent/NL8700397A/nl not_active Application Discontinuation
- 1987-02-18 BE BE8700134A patent/BE1000636A5/fr not_active IP Right Cessation
- 1987-02-18 IT IT19420/87A patent/IT1202565B/it active
Also Published As
| Publication number | Publication date |
|---|---|
| FR2595714A1 (fr) | 1987-09-18 |
| GB2186580A (en) | 1987-08-19 |
| DK77387A (da) | 1987-08-19 |
| US5831022A (en) | 1998-11-03 |
| CH676008A5 (enExample) | 1990-11-30 |
| DK77387D0 (da) | 1987-02-16 |
| GB2186580B (en) | 1990-08-22 |
| FR2595714B1 (fr) | 1990-05-18 |
| BE1000636A5 (fr) | 1989-02-28 |
| GB8703663D0 (en) | 1987-03-25 |
| JP2590085B2 (ja) | 1997-03-12 |
| IT1202565B (it) | 1989-02-09 |
| IT8719420A0 (it) | 1987-02-18 |
| DE3704868A1 (de) | 1987-08-20 |
| DK171419B1 (da) | 1996-10-21 |
| DE3704868C2 (de) | 1995-09-21 |
| JPS62209097A (ja) | 1987-09-14 |
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Legal Events
| Date | Code | Title | Description |
|---|---|---|---|
| CNR | Transfer of rights (patent application after its laying open for public inspection) |
Free format text: HOFFMANN-LA ROCHE AG. F. - |
|
| BA | A request for search or an international-type search has been filed | ||
| BB | A search report has been drawn up | ||
| BC | A request for examination has been filed | ||
| BV | The patent application has lapsed |