KR900005279B1 - 변성 단백질을 복원하는 방법 - Google Patents
변성 단백질을 복원하는 방법 Download PDFInfo
- Publication number
- KR900005279B1 KR900005279B1 KR1019870003281A KR870003281A KR900005279B1 KR 900005279 B1 KR900005279 B1 KR 900005279B1 KR 1019870003281 A KR1019870003281 A KR 1019870003281A KR 870003281 A KR870003281 A KR 870003281A KR 900005279 B1 KR900005279 B1 KR 900005279B1
- Authority
- KR
- South Korea
- Prior art keywords
- protein
- reactivation
- denatured protein
- concentration
- liter
- Prior art date
- Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
- Expired
Links
- 102000004169 proteins and genes Human genes 0.000 title claims description 78
- 108090000623 proteins and genes Proteins 0.000 title claims description 78
- 238000000034 method Methods 0.000 claims description 31
- 239000000243 solution Substances 0.000 claims description 20
- 230000015572 biosynthetic process Effects 0.000 claims description 18
- 239000007853 buffer solution Substances 0.000 claims description 12
- 239000013067 intermediate product Substances 0.000 claims description 8
- 239000000203 mixture Substances 0.000 claims description 4
- 238000004090 dissolution Methods 0.000 claims description 3
- 239000012460 protein solution Substances 0.000 claims description 3
- 230000000779 depleting effect Effects 0.000 claims 1
- 235000018102 proteins Nutrition 0.000 description 63
- 230000007420 reactivation Effects 0.000 description 62
- VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 25
- 102000016943 Muramidase Human genes 0.000 description 15
- 108010014251 Muramidase Proteins 0.000 description 15
- 108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 description 15
- 238000005755 formation reaction Methods 0.000 description 15
- 229960000274 lysozyme Drugs 0.000 description 15
- 235000010335 lysozyme Nutrition 0.000 description 15
- 239000004325 lysozyme Substances 0.000 description 15
- 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 14
- 239000000872 buffer Substances 0.000 description 14
- 229960001484 edetic acid Drugs 0.000 description 14
- 230000010349 pulsation Effects 0.000 description 13
- RWSXRVCMGQZWBV-WDSKDSINSA-N glutathione Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@@H](CS)C(=O)NCC(O)=O RWSXRVCMGQZWBV-WDSKDSINSA-N 0.000 description 12
- 238000005259 measurement Methods 0.000 description 11
- 238000010405 reoxidation reaction Methods 0.000 description 11
- 238000004925 denaturation Methods 0.000 description 10
- 230000036425 denaturation Effects 0.000 description 10
- 230000000694 effects Effects 0.000 description 10
- LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 10
- 108010088350 Lactate Dehydrogenase 5 Proteins 0.000 description 9
- 238000011084 recovery Methods 0.000 description 9
- 102100034671 L-lactate dehydrogenase A chain Human genes 0.000 description 8
- VHJLVAABSRFDPM-ZXZARUISSA-N dithioerythritol Chemical compound SC[C@H](O)[C@H](O)CS VHJLVAABSRFDPM-ZXZARUISSA-N 0.000 description 8
- 239000000543 intermediate Substances 0.000 description 8
- 102000004190 Enzymes Human genes 0.000 description 7
- 108090000790 Enzymes Proteins 0.000 description 7
- 108010053070 Glutathione Disulfide Proteins 0.000 description 7
- 239000007983 Tris buffer Substances 0.000 description 7
- 238000006243 chemical reaction Methods 0.000 description 7
- 229940088598 enzyme Drugs 0.000 description 7
- YPZRWBKMTBYPTK-BJDJZHNGSA-N glutathione disulfide Chemical compound OC(=O)[C@@H](N)CCC(=O)N[C@H](C(=O)NCC(O)=O)CSSC[C@@H](C(=O)NCC(O)=O)NC(=O)CC[C@H](N)C(O)=O YPZRWBKMTBYPTK-BJDJZHNGSA-N 0.000 description 7
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 7
- 238000010586 diagram Methods 0.000 description 6
- 230000009467 reduction Effects 0.000 description 6
- 238000010790 dilution Methods 0.000 description 5
- 239000012895 dilution Substances 0.000 description 5
- 229960003180 glutathione Drugs 0.000 description 5
- 229910000160 potassium phosphate Inorganic materials 0.000 description 5
- 235000011009 potassium phosphates Nutrition 0.000 description 5
- NBIIXXVUZAFLBC-UHFFFAOYSA-N Phosphoric acid Chemical compound OP(O)(O)=O NBIIXXVUZAFLBC-UHFFFAOYSA-N 0.000 description 4
- 238000002474 experimental method Methods 0.000 description 4
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 3
- 229930064664 L-arginine Natural products 0.000 description 3
- 235000014852 L-arginine Nutrition 0.000 description 3
- 102100033571 Tissue-type plasminogen activator Human genes 0.000 description 3
- 238000010521 absorption reaction Methods 0.000 description 3
- 239000002253 acid Substances 0.000 description 3
- 230000000052 comparative effect Effects 0.000 description 3
- 238000011437 continuous method Methods 0.000 description 3
- 238000002156 mixing Methods 0.000 description 3
- 238000002360 preparation method Methods 0.000 description 3
- 101710088194 Dehydrogenase Proteins 0.000 description 2
- 108010024636 Glutathione Proteins 0.000 description 2
- 108050006955 Tissue-type plasminogen activator Proteins 0.000 description 2
- 229910000147 aluminium phosphate Inorganic materials 0.000 description 2
- 230000004071 biological effect Effects 0.000 description 2
- 210000002421 cell wall Anatomy 0.000 description 2
- 238000005119 centrifugation Methods 0.000 description 2
- 230000003247 decreasing effect Effects 0.000 description 2
- 229960000789 guanidine hydrochloride Drugs 0.000 description 2
- PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 description 2
- 229910001385 heavy metal Inorganic materials 0.000 description 2
- 239000012535 impurity Substances 0.000 description 2
- JVTAAEKCZFNVCJ-UHFFFAOYSA-N lactic acid Chemical compound CC(O)C(O)=O JVTAAEKCZFNVCJ-UHFFFAOYSA-N 0.000 description 2
- 238000004519 manufacturing process Methods 0.000 description 2
- 230000008569 process Effects 0.000 description 2
- 230000017854 proteolysis Effects 0.000 description 2
- 238000000926 separation method Methods 0.000 description 2
- 238000003860 storage Methods 0.000 description 2
- 239000000725 suspension Substances 0.000 description 2
- 230000007704 transition Effects 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
- BWGNESOTFCXPMA-UHFFFAOYSA-N Dihydrogen disulfide Chemical compound SS BWGNESOTFCXPMA-UHFFFAOYSA-N 0.000 description 1
- 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 1
- OUYCCCASQSFEME-QMMMGPOBSA-N L-tyrosine Chemical compound OC(=O)[C@@H](N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-QMMMGPOBSA-N 0.000 description 1
- GUBGYTABKSRVRQ-QKKXKWKRSA-N Lactose Natural products OC[C@H]1O[C@@H](O[C@H]2[C@H](O)[C@@H](O)C(O)O[C@@H]2CO)[C@H](O)[C@@H](O)[C@H]1O GUBGYTABKSRVRQ-QKKXKWKRSA-N 0.000 description 1
- WHXSMMKQMYFTQS-UHFFFAOYSA-N Lithium Chemical compound [Li] WHXSMMKQMYFTQS-UHFFFAOYSA-N 0.000 description 1
- 101710157833 Lysozyme A Proteins 0.000 description 1
- 241000191938 Micrococcus luteus Species 0.000 description 1
- 229920005654 Sephadex Polymers 0.000 description 1
- 239000012507 Sephadex™ Substances 0.000 description 1
- 102000007562 Serum Albumin Human genes 0.000 description 1
- 108010071390 Serum Albumin Proteins 0.000 description 1
- 108090000373 Tissue Plasminogen Activator Proteins 0.000 description 1
- QIVBCDIJIAJPQS-UHFFFAOYSA-N Tryptophan Natural products C1=CC=C2C(CC(N)C(O)=O)=CNC2=C1 QIVBCDIJIAJPQS-UHFFFAOYSA-N 0.000 description 1
- 239000006035 Tryptophane Substances 0.000 description 1
- 230000002378 acidificating effect Effects 0.000 description 1
- 230000009471 action Effects 0.000 description 1
- 230000004913 activation Effects 0.000 description 1
- 150000001413 amino acids Chemical group 0.000 description 1
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 1
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 1
- 235000011130 ammonium sulphate Nutrition 0.000 description 1
- 125000003118 aryl group Chemical group 0.000 description 1
- 230000008827 biological function Effects 0.000 description 1
- 244000309466 calf Species 0.000 description 1
- 238000011088 calibration curve Methods 0.000 description 1
- 230000006037 cell lysis Effects 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 230000009918 complex formation Effects 0.000 description 1
- 150000001875 compounds Chemical class 0.000 description 1
- XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 description 1
- 235000018417 cysteine Nutrition 0.000 description 1
- 230000007423 decrease Effects 0.000 description 1
- 238000011033 desalting Methods 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- 230000007717 exclusion Effects 0.000 description 1
- 230000001747 exhibiting effect Effects 0.000 description 1
- 238000000605 extraction Methods 0.000 description 1
- 238000001914 filtration Methods 0.000 description 1
- 238000004108 freeze drying Methods 0.000 description 1
- 238000002523 gelfiltration Methods 0.000 description 1
- 238000007429 general method Methods 0.000 description 1
- 238000010353 genetic engineering Methods 0.000 description 1
- 229940045883 glutathione disulfide Drugs 0.000 description 1
- 230000002209 hydrophobic effect Effects 0.000 description 1
- 238000011534 incubation Methods 0.000 description 1
- 239000004310 lactic acid Substances 0.000 description 1
- 235000014655 lactic acid Nutrition 0.000 description 1
- 239000008101 lactose Substances 0.000 description 1
- 229910052744 lithium Inorganic materials 0.000 description 1
- 239000000463 material Substances 0.000 description 1
- 230000004048 modification Effects 0.000 description 1
- 238000012986 modification Methods 0.000 description 1
- 239000002808 molecular sieve Substances 0.000 description 1
- 210000003205 muscle Anatomy 0.000 description 1
- 239000012299 nitrogen atmosphere Substances 0.000 description 1
- 230000001590 oxidative effect Effects 0.000 description 1
- YPZRWBKMTBYPTK-UHFFFAOYSA-N oxidized gamma-L-glutamyl-L-cysteinylglycine Natural products OC(=O)C(N)CCC(=O)NC(C(=O)NCC(O)=O)CSSCC(C(=O)NCC(O)=O)NC(=O)CCC(N)C(O)=O YPZRWBKMTBYPTK-UHFFFAOYSA-N 0.000 description 1
- 239000008188 pellet Substances 0.000 description 1
- 239000008363 phosphate buffer Substances 0.000 description 1
- 230000010287 polarization Effects 0.000 description 1
- OTYBMLCTZGSZBG-UHFFFAOYSA-L potassium sulfate Chemical compound [K+].[K+].[O-]S([O-])(=O)=O OTYBMLCTZGSZBG-UHFFFAOYSA-L 0.000 description 1
- 229910052939 potassium sulfate Inorganic materials 0.000 description 1
- 235000011151 potassium sulphates Nutrition 0.000 description 1
- 230000005451 protein repair Effects 0.000 description 1
- 238000007100 recyclization reaction Methods 0.000 description 1
- 238000005067 remediation Methods 0.000 description 1
- 239000012465 retentate Substances 0.000 description 1
- 230000035945 sensitivity Effects 0.000 description 1
- 238000012163 sequencing technique Methods 0.000 description 1
- 238000007086 side reaction Methods 0.000 description 1
- 238000010334 sieve classification Methods 0.000 description 1
- URGAHOPLAPQHLN-UHFFFAOYSA-N sodium aluminosilicate Chemical compound [Na+].[Al+3].[O-][Si]([O-])=O.[O-][Si]([O-])=O URGAHOPLAPQHLN-UHFFFAOYSA-N 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 239000002904 solvent Substances 0.000 description 1
- 239000007858 starting material Substances 0.000 description 1
- 230000000638 stimulation Effects 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000012085 test solution Substances 0.000 description 1
- 238000012360 testing method Methods 0.000 description 1
- 229960004799 tryptophan Drugs 0.000 description 1
- OUYCCCASQSFEME-UHFFFAOYSA-N tyrosine Natural products OC(=O)C(N)CC1=CC=C(O)C=C1 OUYCCCASQSFEME-UHFFFAOYSA-N 0.000 description 1
- 238000000108 ultra-filtration Methods 0.000 description 1
- 238000005406 washing Methods 0.000 description 1
Images
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
- C12N9/00—Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
- C12N9/96—Stabilising an enzyme by forming an adduct or a composition; Forming enzyme conjugates
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/24—Hydrolases (3) acting on glycosyl compounds (3.2)
- C12N9/2402—Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
- C12N9/2462—Lysozyme (3.2.1.17)
-
- 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
- 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
- C12N9/0004—Oxidoreductases (1.)
- C12N9/0006—Oxidoreductases (1.) acting on CH-OH groups as donors (1.1)
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
-
- 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
- C12N9/14—Hydrolases (3)
- C12N9/48—Hydrolases (3) acting on peptide bonds (3.4)
- C12N9/50—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25)
- C12N9/64—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue
- C12N9/6421—Proteinases, e.g. Endopeptidases (3.4.21-3.4.25) derived from animal tissue from mammals
- C12N9/6424—Serine endopeptidases (3.4.21)
- C12N9/6456—Plasminogen activators
- C12N9/6459—Plasminogen activators t-plasminogen activator (3.4.21.68), i.e. tPA
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Y—ENZYMES
- C12Y304/00—Hydrolases acting on peptide bonds, i.e. peptidases (3.4)
- C12Y304/21—Serine endopeptidases (3.4.21)
- C12Y304/21069—Protein C activated (3.4.21.69)
Landscapes
- Chemical & Material Sciences (AREA)
- Health & Medical Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Genetics & Genomics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Molecular Biology (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Biomedical Technology (AREA)
- Biotechnology (AREA)
- Microbiology (AREA)
- Analytical Chemistry (AREA)
- General Chemical & Material Sciences (AREA)
- Biophysics (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Crystallography & Structural Chemistry (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Peptides Or Proteins (AREA)
- Preparation Of Compounds By Using Micro-Organisms (AREA)
- Enzymes And Modification Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| DE3611817.6 | 1986-04-08 | ||
| DE19863611817 DE3611817A1 (de) | 1986-04-08 | 1986-04-08 | Verfahren zur renaturierung von proteinen |
| DEP3611817.6 | 1986-04-08 |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR870010185A KR870010185A (ko) | 1987-11-30 |
| KR900005279B1 true KR900005279B1 (ko) | 1990-07-27 |
Family
ID=6298240
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| KR1019870003281A Expired KR900005279B1 (ko) | 1986-04-08 | 1987-04-07 | 변성 단백질을 복원하는 방법 |
Country Status (20)
| Country | Link |
|---|---|
| US (1) | US4933434A (https=) |
| EP (1) | EP0241022B1 (https=) |
| JP (1) | JPH0742307B2 (https=) |
| KR (1) | KR900005279B1 (https=) |
| AT (1) | ATE84541T1 (https=) |
| AU (1) | AU583723B2 (https=) |
| CA (1) | CA1304191C (https=) |
| CZ (1) | CZ283304B6 (https=) |
| DD (1) | DD260280A5 (https=) |
| DE (2) | DE3611817A1 (https=) |
| DK (1) | DK173650B1 (https=) |
| ES (1) | ES2038969T3 (https=) |
| FI (1) | FI93842C (https=) |
| GR (1) | GR3007605T3 (https=) |
| HK (1) | HK46896A (https=) |
| HU (1) | HU198514B (https=) |
| IE (1) | IE60064B1 (https=) |
| IL (1) | IL82091A (https=) |
| SK (1) | SK279976B6 (https=) |
| ZA (1) | ZA872474B (https=) |
Families Citing this family (15)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| WO1989001484A1 (fr) * | 1987-08-14 | 1989-02-23 | Gebro Broschek Kg Pharmazeutische Fabrik | Procede d'oxydation intramoleculaire de deux groupes -sh dans un compose peptidique de façon a former un pont bisulfure et peptide produit selon ce procede |
| DE3832898A1 (de) * | 1988-09-28 | 1990-04-12 | Boehringer Mannheim Gmbh | Praeparat von in prokaryonten exprimiertem plasminogenaktivator |
| DE3835350A1 (de) * | 1988-10-17 | 1990-04-19 | Boehringer Mannheim Gmbh | Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern |
| DE3903581A1 (de) * | 1989-02-07 | 1990-08-16 | Boehringer Mannheim Gmbh | Gewebs-plasminogenaktivator-derivat |
| JPH06500084A (ja) * | 1990-08-20 | 1994-01-06 | ノボ ノルディスク アクティーゼルスカブ | 生物学的に活性な化合物、その製造方法及びその利用 |
| AU664021B2 (en) * | 1990-09-05 | 1995-11-02 | Natinco Nv | Solubilization of proteins in active forms |
| US5023323A (en) * | 1990-09-12 | 1991-06-11 | Monsanto Company | Method of somatotropin naturation |
| DE4037196A1 (de) * | 1990-11-22 | 1992-05-27 | Boehringer Mannheim Gmbh | Verfahren zur reaktivierung von denaturiertem protein |
| DE4139000A1 (de) | 1991-11-27 | 1993-06-03 | Boehringer Mannheim Gmbh | Verfahren zur gentechnologischen herstellung von biologisch aktivem ss-ngf |
| EP1077263A1 (de) | 1999-07-29 | 2001-02-21 | F.Hoffmann-La Roche Ag | Verfahren zur Herstellung von natürlich gefalteten und sekretierten Proteinen durch Co-Sekretion von Chaperonen |
| US20050079526A1 (en) * | 2002-02-20 | 2005-04-14 | Affinium Pharmaceuticals, Inc. | Methods and apparatuses for characterizing refolding and aggregation of biological molecules |
| CN102892780B (zh) | 2010-03-17 | 2015-07-29 | 通益制药有限公司 | 获得生物活性的重组人g-csf的方法 |
| WO2012104099A1 (en) | 2011-02-04 | 2012-08-09 | Glucometrix Ag | Process for the production of recombinant trypsin |
| CN106699836A (zh) * | 2017-03-07 | 2017-05-24 | 安徽鑫华坤生物工程有限公司 | 一种蛋白质复性的透析设备 |
| CN120341163B (zh) * | 2025-06-20 | 2025-09-30 | 深圳市中芯辰瑞光电科技有限公司 | 一种固晶头 |
Family Cites Families (13)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US4216141A (en) * | 1978-07-19 | 1980-08-05 | The Salk Institute For Biological Studies | Method for cyclization of peptides |
| DE3231658A1 (https=) | 1981-01-21 | 1983-11-17 | ||
| IE55163B1 (en) * | 1982-06-07 | 1990-06-20 | Celltech Ltd | A process for the preparation of chymosin |
| JPS593711U (ja) * | 1982-06-30 | 1984-01-11 | 協伸工業株式会社 | 電線被覆剥取器 |
| AU538170B2 (en) * | 1982-09-15 | 1984-08-02 | Owens-Illinois Glass Container Inc. | Modified protein to mould an enzyme type molecule |
| GR79124B (https=) * | 1982-12-22 | 1984-10-02 | Genentech Inc | |
| EP0122080B1 (en) * | 1983-03-25 | 1989-09-13 | Celltech Limited | A process for the production of a protein |
| US4530787A (en) * | 1984-03-28 | 1985-07-23 | Cetus Corporation | Controlled oxidation of microbially produced cysteine-containing proteins |
| KR860007688A (ko) | 1985-03-08 | 1986-10-15 | 시끼 모리야 | 전자석장치(電磁石裝置) |
| GB8508340D0 (en) * | 1985-03-29 | 1985-05-09 | Creighton T E | Production of protein |
| EP0208539A3 (en) * | 1985-07-11 | 1988-08-03 | Repligen Corporation | Folding disulfide-cross-linkable proteins |
| US4656255A (en) * | 1985-09-09 | 1987-04-07 | International Minerals & Chemical Corp. | Protein recovery |
| DE3618817A1 (de) * | 1986-06-04 | 1987-12-10 | Behringwerke Ag | Verfahren zur gewinnung aktiver proteine aus einer biologisch inaktiven form |
-
1986
- 1986-04-08 DE DE19863611817 patent/DE3611817A1/de not_active Withdrawn
-
1987
- 1987-03-16 IE IE69587A patent/IE60064B1/en not_active IP Right Cessation
- 1987-04-02 CA CA000533687A patent/CA1304191C/en not_active Expired - Lifetime
- 1987-04-02 IL IL82091A patent/IL82091A/xx not_active IP Right Cessation
- 1987-04-06 JP JP62083132A patent/JPH0742307B2/ja not_active Expired - Lifetime
- 1987-04-06 DD DD87301550A patent/DD260280A5/de not_active IP Right Cessation
- 1987-04-07 CZ CS872495A patent/CZ283304B6/cs not_active IP Right Cessation
- 1987-04-07 KR KR1019870003281A patent/KR900005279B1/ko not_active Expired
- 1987-04-07 ZA ZA872474A patent/ZA872474B/xx unknown
- 1987-04-07 SK SK2495-87A patent/SK279976B6/sk unknown
- 1987-04-07 FI FI871522A patent/FI93842C/fi not_active IP Right Cessation
- 1987-04-07 HU HU871493A patent/HU198514B/hu unknown
- 1987-04-08 DK DK198701797A patent/DK173650B1/da active IP Right Grant
- 1987-04-08 DE DE8787105230T patent/DE3783497D1/de not_active Expired - Lifetime
- 1987-04-08 AT AT87105230T patent/ATE84541T1/de not_active IP Right Cessation
- 1987-04-08 ES ES198787105230T patent/ES2038969T3/es not_active Expired - Lifetime
- 1987-04-08 EP EP87105230A patent/EP0241022B1/de not_active Expired - Lifetime
- 1987-04-08 AU AU71190/87A patent/AU583723B2/en not_active Ceased
-
1989
- 1989-01-13 US US07/298,274 patent/US4933434A/en not_active Expired - Lifetime
-
1993
- 1993-04-09 GR GR920403237T patent/GR3007605T3/el unknown
-
1996
- 1996-03-14 HK HK46896A patent/HK46896A/xx not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| DD260280A5 (de) | 1988-09-21 |
| GR3007605T3 (https=) | 1993-08-31 |
| CA1304191C (en) | 1992-06-23 |
| EP0241022A3 (en) | 1989-10-25 |
| ATE84541T1 (de) | 1993-01-15 |
| CZ249587A3 (en) | 1997-11-12 |
| CZ283304B6 (cs) | 1998-02-18 |
| HK46896A (en) | 1996-03-22 |
| HU198514B (en) | 1989-10-30 |
| DE3783497D1 (de) | 1993-02-25 |
| IL82091A0 (en) | 1987-10-30 |
| IE60064B1 (en) | 1994-06-01 |
| FI871522L (fi) | 1987-10-09 |
| IL82091A (en) | 1991-12-15 |
| AU7119087A (en) | 1987-10-15 |
| SK249587A3 (en) | 1999-06-11 |
| EP0241022A2 (de) | 1987-10-14 |
| EP0241022B1 (de) | 1993-01-13 |
| IE870695L (en) | 1987-10-08 |
| ES2038969T3 (es) | 1993-08-16 |
| FI93842B (fi) | 1995-02-28 |
| US4933434A (en) | 1990-06-12 |
| JPS62242697A (ja) | 1987-10-23 |
| FI871522A0 (fi) | 1987-04-07 |
| DK173650B1 (da) | 2001-05-21 |
| HUT44046A (en) | 1988-01-28 |
| AU583723B2 (en) | 1989-05-04 |
| DK179787D0 (da) | 1987-04-08 |
| DE3611817A1 (de) | 1987-10-15 |
| SK279976B6 (sk) | 1999-06-11 |
| JPH0742307B2 (ja) | 1995-05-10 |
| ZA872474B (en) | 1988-07-27 |
| FI93842C (fi) | 1995-06-12 |
| KR870010185A (ko) | 1987-11-30 |
| DK179787A (da) | 1987-10-09 |
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