IL92012A - A process for activating proteins produced by genetic technology expressed in prokaryotes - Google Patents

A process for activating proteins produced by genetic technology expressed in prokaryotes

Info

Publication number: IL92012A
Authority: IL; Israel
Prior art keywords: litre; process according; mole; concentration; mmole
Prior art date: 1988-10-17

Application number

IL9201289A

Other languages

English (en)

Hebrew (he)

Other versions

IL92012A0 (en

Original Assignee

Boehringer Mannheim Gmbh

Priority date (The priority date 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 date listed.)

1988-10-17

Filing date

1989-10-17

Publication date

1994-12-29

1989-10-17 Application filed by Boehringer Mannheim Gmbh filed Critical Boehringer Mannheim Gmbh

1990-07-12 Publication of IL92012A0 publication Critical patent/IL92012A0/xx

1994-12-29 Publication of IL92012A publication Critical patent/IL92012A/en

Links

108090000623 proteins and genes Proteins 0.000 title claims abstract description 63
102000004169 proteins and genes Human genes 0.000 title claims abstract description 55
241000894006 Bacteria Species 0.000 title claims abstract description 12
230000004913 activation Effects 0.000 title claims abstract description 12
238000000034 method Methods 0.000 title claims description 42
230000008569 process Effects 0.000 title claims description 33
229960000789 guanidine hydrochloride Drugs 0.000 claims abstract description 28
PJJJBBJSCAKJQF-UHFFFAOYSA-N guanidinium chloride Chemical compound [Cl-].NC(N)=[NH2+] PJJJBBJSCAKJQF-UHFFFAOYSA-N 0.000 claims abstract description 28
230000007420 reactivation Effects 0.000 claims abstract description 23
239000000872 buffer Substances 0.000 claims abstract description 18
238000000502 dialysis Methods 0.000 claims abstract description 16
XSQUKJJJFZCRTK-UHFFFAOYSA-N Urea Chemical compound NC(N)=O XSQUKJJJFZCRTK-UHFFFAOYSA-N 0.000 claims abstract description 10
239000004202 carbamide Substances 0.000 claims abstract description 6
235000018102 proteins Nutrition 0.000 claims description 52
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 claims description 49
229960003180 glutathione Drugs 0.000 claims description 24
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 claims description 19
108010053070 Glutathione Disulfide Proteins 0.000 claims description 18
KCXVZYZYPLLWCC-UHFFFAOYSA-N EDTA Chemical compound OC(=O)CN(CC(O)=O)CCN(CC(O)=O)CC(O)=O KCXVZYZYPLLWCC-UHFFFAOYSA-N 0.000 claims description 17
239000003795 chemical substances by application Substances 0.000 claims description 14
239000000243 solution Substances 0.000 claims description 12
239000007983 Tris buffer Substances 0.000 claims description 10
LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 claims description 10
150000001875 compounds Chemical class 0.000 claims description 8
230000029087 digestion Effects 0.000 claims description 8
VHJLVAABSRFDPM-ZXZARUISSA-N dithioerythritol Chemical compound SC[C@H](O)[C@H](O)CS VHJLVAABSRFDPM-ZXZARUISSA-N 0.000 claims description 8
239000003638 chemical reducing agent Substances 0.000 claims description 7
239000004475 Arginine Substances 0.000 claims description 6
108091003079 Bovine Serum Albumin Proteins 0.000 claims description 5
229940098773 bovine serum albumin Drugs 0.000 claims description 5
ZRALSGWEFCBTJO-UHFFFAOYSA-N Guanidine Chemical compound NC(N)=N ZRALSGWEFCBTJO-UHFFFAOYSA-N 0.000 claims description 4
ODKSFYDXXFIFQN-UHFFFAOYSA-N arginine Natural products OC(=O)C(N)CCCNC(N)=N ODKSFYDXXFIFQN-UHFFFAOYSA-N 0.000 claims description 4
108010024636 Glutathione Proteins 0.000 claims description 3
102000016943 Muramidase Human genes 0.000 claims description 3
108010014251 Muramidase Proteins 0.000 claims description 3
108010062010 N-Acetylmuramoyl-L-alanine Amidase Proteins 0.000 claims description 3
229960003121 arginine Drugs 0.000 claims description 3
229960003589 arginine hydrochloride Drugs 0.000 claims description 3
229960000274 lysozyme Drugs 0.000 claims description 3
239000004325 lysozyme Substances 0.000 claims description 3
235000010335 lysozyme Nutrition 0.000 claims description 3
DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 3
108010021625 Immunoglobulin Fragments Proteins 0.000 claims description 2
102000008394 Immunoglobulin Fragments Human genes 0.000 claims description 2
CHJJGSNFBQVOTG-UHFFFAOYSA-N N-methyl-guanidine Natural products CNC(N)=N CHJJGSNFBQVOTG-UHFFFAOYSA-N 0.000 claims description 2
230000002378 acidificating effect Effects 0.000 claims description 2
235000018417 cysteine Nutrition 0.000 claims description 2
XUJNEKJLAYXESH-UHFFFAOYSA-N cysteine Natural products SCC(N)C(O)=O XUJNEKJLAYXESH-UHFFFAOYSA-N 0.000 claims description 2
SWSQBOPZIKWTGO-UHFFFAOYSA-N dimethylaminoamidine Natural products CN(C)C(N)=N SWSQBOPZIKWTGO-UHFFFAOYSA-N 0.000 claims description 2
239000006185 dispersion Substances 0.000 claims description 2
229960004198 guanidine Drugs 0.000 claims description 2
230000007935 neutral effect Effects 0.000 claims description 2
239000012062 aqueous buffer Substances 0.000 claims 2
125000004435 hydrogen atom Chemical group [H]* 0.000 claims 2
OKTJSMMVPCPJKN-UHFFFAOYSA-N Carbon Chemical compound [C] OKTJSMMVPCPJKN-UHFFFAOYSA-N 0.000 claims 1
XUJNEKJLAYXESH-REOHCLBHSA-N L-Cysteine Chemical compound SC[C@H](N)C(O)=O XUJNEKJLAYXESH-REOHCLBHSA-N 0.000 claims 1
ODKSFYDXXFIFQN-BYPYZUCNSA-P L-argininium(2+) Chemical compound NC(=[NH2+])NCCC[C@H]([NH3+])C(O)=O ODKSFYDXXFIFQN-BYPYZUCNSA-P 0.000 claims 1
229910052799 carbon Inorganic materials 0.000 claims 1
229940045883 glutathione disulfide Drugs 0.000 claims 1
125000003396 thiol group Chemical group [H]S* 0.000 claims 1
238000012360 testing method Methods 0.000 description 14
210000004027 cell Anatomy 0.000 description 13
241000588724 Escherichia coli Species 0.000 description 12
239000012634 fragment Substances 0.000 description 12
210000003000 inclusion body Anatomy 0.000 description 11
VEXZGXHMUGYJMC-UHFFFAOYSA-N Hydrochloric acid Chemical compound Cl VEXZGXHMUGYJMC-UHFFFAOYSA-N 0.000 description 10
230000000694 effects Effects 0.000 description 9
239000013612 plasmid Substances 0.000 description 9
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 8
230000009467 reduction Effects 0.000 description 8
108010054477 Immunoglobulin Fab Fragments Proteins 0.000 description 7
102000001706 Immunoglobulin Fab Fragments Human genes 0.000 description 7
230000015572 biosynthetic process Effects 0.000 description 7
238000006243 chemical reaction Methods 0.000 description 7
238000001514 detection method Methods 0.000 description 7
230000005764 inhibitory process Effects 0.000 description 7
239000008188 pellet Substances 0.000 description 7
QTBSBXVTEAMEQO-UHFFFAOYSA-N Acetic acid Chemical compound CC(O)=O QTBSBXVTEAMEQO-UHFFFAOYSA-N 0.000 description 6
229940088598 enzyme Drugs 0.000 description 6
238000010405 reoxidation reaction Methods 0.000 description 6
102000004420 Creatine Kinase Human genes 0.000 description 5
108010042126 Creatine kinase Proteins 0.000 description 5
ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 5
102000004190 Enzymes Human genes 0.000 description 4
108090000790 Enzymes Proteins 0.000 description 4
241001494479 Pecora Species 0.000 description 4
FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 4
239000002299 complementary DNA Substances 0.000 description 4
238000010790 dilution Methods 0.000 description 4
239000012895 dilution Substances 0.000 description 4
239000002773 nucleotide Substances 0.000 description 4
125000003729 nucleotide group Chemical group 0.000 description 4
238000007254 oxidation reaction Methods 0.000 description 4
238000002360 preparation method Methods 0.000 description 4
108010044467 Isoenzymes Proteins 0.000 description 3
229930064664 L-arginine Natural products 0.000 description 3
235000014852 L-arginine Nutrition 0.000 description 3
HEMHJVSKTPXQMS-UHFFFAOYSA-M Sodium hydroxide Chemical compound [OH-].[Na+] HEMHJVSKTPXQMS-UHFFFAOYSA-M 0.000 description 3
229920004890 Triton X-100 Polymers 0.000 description 3
239000013504 Triton X-100 Substances 0.000 description 3
235000001014 amino acid Nutrition 0.000 description 3
150000001413 amino acids Chemical class 0.000 description 3
238000001212 derivatisation Methods 0.000 description 3
230000002255 enzymatic effect Effects 0.000 description 3
239000013613 expression plasmid Substances 0.000 description 3
238000011534 incubation Methods 0.000 description 3
238000005259 measurement Methods 0.000 description 3
230000003647 oxidation Effects 0.000 description 3
210000002027 skeletal muscle Anatomy 0.000 description 3
XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 3
108020004705 Codon Proteins 0.000 description 2
NBSCHQHZLSJFNQ-GASJEMHNSA-N D-Glucose 6-phosphate Chemical compound OC1O[C@H](COP(O)(O)=O)[C@@H](O)[C@H](O)[C@H]1O NBSCHQHZLSJFNQ-GASJEMHNSA-N 0.000 description 2
VFRROHXSMXFLSN-UHFFFAOYSA-N Glc6P Natural products OP(=O)(O)OCC(O)C(O)C(O)C(O)C=O VFRROHXSMXFLSN-UHFFFAOYSA-N 0.000 description 2
DHMQDGOQFOQNFH-UHFFFAOYSA-N Glycine Chemical compound NCC(O)=O DHMQDGOQFOQNFH-UHFFFAOYSA-N 0.000 description 2
108060003951 Immunoglobulin Proteins 0.000 description 2
LSDPWZHWYPCBBB-UHFFFAOYSA-N Methanethiol Chemical group SC LSDPWZHWYPCBBB-UHFFFAOYSA-N 0.000 description 2
DRBBFCLWYRJSJZ-UHFFFAOYSA-N N-phosphocreatine Chemical compound OC(=O)CN(C)C(=N)NP(O)(O)=O DRBBFCLWYRJSJZ-UHFFFAOYSA-N 0.000 description 2
XJLXINKUBYWONI-DQQFMEOOSA-N [[(2r,3r,4r,5r)-5-(6-aminopurin-9-yl)-3-hydroxy-4-phosphonooxyoxolan-2-yl]methoxy-hydroxyphosphoryl] [(2s,3r,4s,5s)-5-(3-carbamoylpyridin-1-ium-1-yl)-3,4-dihydroxyoxolan-2-yl]methyl phosphate Chemical compound NC(=O)C1=CC=C[N+]([C@@H]2[C@H]([C@@H](O)[C@H](COP([O-])(=O)OP(O)(=O)OC[C@@H]3[C@H]([C@@H](OP(O)(O)=O)[C@@H](O3)N3C4=NC=NC(N)=C4N=C3)O)O2)O)=C1 XJLXINKUBYWONI-DQQFMEOOSA-N 0.000 description 2
230000009471 action Effects 0.000 description 2
229940024606 amino acid Drugs 0.000 description 2
239000000427 antigen Substances 0.000 description 2
102000036639 antigens Human genes 0.000 description 2
108091007433 antigens Proteins 0.000 description 2
OHDRQQURAXLVGJ-HLVWOLMTSA-N azane;(2e)-3-ethyl-2-[(e)-(3-ethyl-6-sulfo-1,3-benzothiazol-2-ylidene)hydrazinylidene]-1,3-benzothiazole-6-sulfonic acid Chemical compound [NH4+].[NH4+].S/1C2=CC(S([O-])(=O)=O)=CC=C2N(CC)C\1=N/N=C1/SC2=CC(S([O-])(=O)=O)=CC=C2N1CC OHDRQQURAXLVGJ-HLVWOLMTSA-N 0.000 description 2
230000003196 chaotropic effect Effects 0.000 description 2
239000003593 chromogenic compound Substances 0.000 description 2
238000003776 cleavage reaction Methods 0.000 description 2
238000010367 cloning Methods 0.000 description 2
238000010276 construction Methods 0.000 description 2
CVSVTCORWBXHQV-UHFFFAOYSA-N creatine Chemical compound NC(=[NH2+])N(C)CC([O-])=O CVSVTCORWBXHQV-UHFFFAOYSA-N 0.000 description 2
VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 2
102000018358 immunoglobulin Human genes 0.000 description 2
238000004519 manufacturing process Methods 0.000 description 2
239000000203 mixture Substances 0.000 description 2
238000011533 pre-incubation Methods 0.000 description 2
230000009257 reactivity Effects 0.000 description 2
230000007017 scission Effects 0.000 description 2
238000010008 shearing Methods 0.000 description 2
239000011780 sodium chloride Substances 0.000 description 2
238000010998 test method Methods 0.000 description 2
LWIHDJKSTIGBAC-UHFFFAOYSA-K tripotassium phosphate Chemical compound [K+].[K+].[K+].[O-]P([O-])([O-])=O LWIHDJKSTIGBAC-UHFFFAOYSA-K 0.000 description 2
102100031126 6-phosphogluconolactonase Human genes 0.000 description 1
108010029731 6-phosphogluconolactonase Proteins 0.000 description 1
108010032595 Antibody Binding Sites Proteins 0.000 description 1
108010054576 Deoxyribonuclease EcoRI Proteins 0.000 description 1
238000002965 ELISA Methods 0.000 description 1
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 1
108010018962 Glucosephosphate Dehydrogenase Proteins 0.000 description 1
239000004471 Glycine Substances 0.000 description 1
102000005548 Hexokinase Human genes 0.000 description 1
108700040460 Hexokinases Proteins 0.000 description 1
108010054278 Lac Repressors Proteins 0.000 description 1
241001465754 Metazoa Species 0.000 description 1
241001529936 Murinae Species 0.000 description 1
NTNWOCRCBQPEKQ-YFKPBYRVSA-N N(omega)-methyl-L-arginine Chemical compound CN=C(N)NCCC[C@H](N)C(O)=O NTNWOCRCBQPEKQ-YFKPBYRVSA-N 0.000 description 1
229910019142 PO4 Inorganic materials 0.000 description 1
241000577979 Peromyscus spicilegus Species 0.000 description 1
108091023045 Untranslated Region Proteins 0.000 description 1
241001672648 Vieira Species 0.000 description 1
238000010521 absorption reaction Methods 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
239000001166 ammonium sulphate Substances 0.000 description 1
235000011130 ammonium sulphate Nutrition 0.000 description 1
238000004458 analytical method Methods 0.000 description 1
235000009697 arginine Nutrition 0.000 description 1
QVGXLLKOCUKJST-UHFFFAOYSA-N atomic oxygen Chemical compound [O] QVGXLLKOCUKJST-UHFFFAOYSA-N 0.000 description 1
230000008033 biological extinction Effects 0.000 description 1
239000007853 buffer solution Substances 0.000 description 1
238000011088 calibration curve Methods 0.000 description 1
230000015556 catabolic process Effects 0.000 description 1
230000008859 change Effects 0.000 description 1
230000000052 comparative effect Effects 0.000 description 1
230000000295 complement effect Effects 0.000 description 1
229960003624 creatine Drugs 0.000 description 1
239000006046 creatine Substances 0.000 description 1
239000003599 detergent Substances 0.000 description 1
238000005516 engineering process Methods 0.000 description 1
238000011049 filling Methods 0.000 description 1
238000001914 filtration Methods 0.000 description 1
238000005194 fractionation Methods 0.000 description 1
239000008103 glucose Substances 0.000 description 1
210000004408 hybridoma Anatomy 0.000 description 1
230000006872 improvement Effects 0.000 description 1
230000002401 inhibitory effect Effects 0.000 description 1
238000004255 ion exchange chromatography Methods 0.000 description 1
239000000463 material Substances 0.000 description 1
244000005700 microbiome Species 0.000 description 1
229930027945 nicotinamide-adenine dinucleotide Natural products 0.000 description 1
108020004707 nucleic acids Proteins 0.000 description 1
102000039446 nucleic acids Human genes 0.000 description 1
150000007523 nucleic acids Chemical class 0.000 description 1
230000003287 optical effect Effects 0.000 description 1
239000001301 oxygen Substances 0.000 description 1
229910052760 oxygen Inorganic materials 0.000 description 1
239000010452 phosphate Substances 0.000 description 1
239000008055 phosphate buffer solution Substances 0.000 description 1
230000026731 phosphorylation Effects 0.000 description 1
238000006366 phosphorylation reaction Methods 0.000 description 1
229910000160 potassium phosphate Inorganic materials 0.000 description 1
235000011009 potassium phosphates Nutrition 0.000 description 1
239000002244 precipitate Substances 0.000 description 1
230000002265 prevention Effects 0.000 description 1
238000011165 process development Methods 0.000 description 1
230000002797 proteolythic effect Effects 0.000 description 1
238000011160 research Methods 0.000 description 1
108091008146 restriction endonucleases Proteins 0.000 description 1
229920006395 saturated elastomer Polymers 0.000 description 1
238000000926 separation method Methods 0.000 description 1
238000004904 shortening Methods 0.000 description 1
238000002741 site-directed mutagenesis Methods 0.000 description 1
238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
230000006641 stabilisation Effects 0.000 description 1
239000003774 sulfhydryl reagent Substances 0.000 description 1
239000000725 suspension Substances 0.000 description 1
GPRLSGONYQIRFK-MNYXATJNSA-N triton Chemical compound [3H+] GPRLSGONYQIRFK-MNYXATJNSA-N 0.000 description 1
238000005406 washing Methods 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
- 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
- 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
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12P—FERMENTATION OR ENZYME-USING PROCESSES TO SYNTHESISE A DESIRED CHEMICAL COMPOUND OR COMPOSITION OR TO SEPARATE OPTICAL ISOMERS FROM A RACEMIC MIXTURE
- C12P19/00—Preparation of compounds containing saccharide radicals
- C12P19/26—Preparation of nitrogen-containing carbohydrates
- C12P19/28—N-glycosides
- C12P19/30—Nucleotides
- C12P19/34—Polynucleotides, e.g. nucleic acids, oligoribonucleotides
- 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)
- 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
- Y10S530/00—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof
- Y10S530/867—Chemistry: natural resins or derivatives; peptides or proteins; lignins or reaction products thereof involving immunoglobulin or antibody produced via recombinant dna technology

Landscapes

Chemical & Material Sciences (AREA)
Health & Medical Sciences (AREA)
Organic Chemistry (AREA)
Life Sciences & Earth Sciences (AREA)
Engineering & Computer Science (AREA)
Genetics & Genomics (AREA)
Zoology (AREA)
Wood Science & Technology (AREA)
Bioinformatics & Cheminformatics (AREA)
Biochemistry (AREA)
General Health & Medical Sciences (AREA)
General Engineering & Computer Science (AREA)
Molecular Biology (AREA)
Biomedical Technology (AREA)
Chemical Kinetics & Catalysis (AREA)
Biotechnology (AREA)
Microbiology (AREA)
Medicinal Chemistry (AREA)
Biophysics (AREA)
General Chemical & Material Sciences (AREA)
Proteomics, Peptides & Aminoacids (AREA)
Analytical Chemistry (AREA)
Physics & Mathematics (AREA)
Plant Pathology (AREA)
Preparation Of Compounds By Using Micro-Organisms (AREA)
Peptides Or Proteins (AREA)
Enzymes And Modification Thereof (AREA)
Saccharide Compounds (AREA)

IL9201289A 1988-10-17 1989-10-17 A process for activating proteins produced by genetic technology expressed in prokaryotes IL92012A (en)

Applications Claiming Priority (1)

Application Number	Priority Date	Filing Date	Title
DE3835350A DE3835350A1 (de)	1988-10-17	1988-10-17	Aktivierung von gentechnologisch hergestellten, in prokaryonten exprimierten antikoerpern

Publications (2)

Publication Number	Publication Date
IL92012A0 IL92012A0 (en)	1990-07-12
IL92012A true IL92012A (en)	1994-12-29

Family

ID=6365312

Family Applications (1)

Application Number	Title	Priority Date	Filing Date
IL9201289A IL92012A (en)	1988-10-17	1989-10-17	A process for activating proteins produced by genetic technology expressed in prokaryotes

Country Status (12)

Country	Link
US (1)	US5077392A (fr)
EP (1)	EP0364926B1 (fr)
JP (1)	JPH0793879B2 (fr)
KR (1)	KR920010873B1 (fr)
AT (1)	ATE101650T1 (fr)
AU (1)	AU609645B2 (fr)
CA (1)	CA2000604C (fr)
DD (1)	DD285613A5 (fr)
DE (2)	DE3835350A1 (fr)
DK (1)	DK175439B1 (fr)
ES (1)	ES2061876T3 (fr)
IL (1)	IL92012A (fr)

Families Citing this family (28)

* Cited by examiner, † Cited by third party
Publication number	Priority date	Publication date	Assignee	Title
US5453363A (en) *	1985-10-23	1995-09-26	Boehringer Mannheim Gmbh	Process for the activation of t-PA or Ing after genetic expression in prokaryotes
US5676947A (en) *	1989-02-07	1997-10-14	Boehringer Manneheim Gmbh	Method for treating thromboembolic conditions using thrombolytically active proteins
DE4037196A1 (de) *	1990-11-22	1992-05-27	Boehringer Mannheim Gmbh	Verfahren zur reaktivierung von denaturiertem protein
DE4105480A1 (de) *	1991-02-21	1992-08-27	Boehringer Mannheim Gmbh	Verbesserte aktivierung von rekombinanten proteinen
AU3812993A (en) *	1992-03-24	1993-10-21	Synergen, Inc.	Refolding and purification of insulin-like growth factor I
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1988
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1989
- 1989-10-13 CA CA002000604A patent/CA2000604C/fr not_active Expired - Lifetime
- 1989-10-16 ES ES89119181T patent/ES2061876T3/es not_active Expired - Lifetime
- 1989-10-16 EP EP89119181A patent/EP0364926B1/fr not_active Expired - Lifetime
- 1989-10-16 AT AT89119181T patent/ATE101650T1/de not_active IP Right Cessation
- 1989-10-16 DD DD89333621A patent/DD285613A5/de not_active IP Right Cessation
- 1989-10-16 DE DE89119181T patent/DE58906984D1/de not_active Expired - Lifetime
- 1989-10-16 AU AU42931/89A patent/AU609645B2/en not_active Expired
- 1989-10-17 IL IL9201289A patent/IL92012A/en not_active IP Right Cessation
- 1989-10-17 DK DK198905159A patent/DK175439B1/da not_active IP Right Cessation
- 1989-10-17 KR KR1019890014951A patent/KR920010873B1/ko not_active Expired
- 1989-10-17 US US07/422,948 patent/US5077392A/en not_active Expired - Lifetime
- 1989-10-17 JP JP1268298A patent/JPH0793879B2/ja not_active Expired - Lifetime

Also Published As

Publication number	Publication date
IL92012A0 (en)	1990-07-12
KR900006515A (ko)	1990-05-08
DD285613A5 (de)	1990-12-19
AU4293189A (en)	1990-04-26
EP0364926B1 (fr)	1994-02-16
DK175439B1 (da)	2004-10-18
US5077392A (en)	1991-12-31
DE58906984D1 (de)	1994-03-24
JPH02227090A (ja)	1990-09-10
DE3835350A1 (de)	1990-04-19
CA2000604A1 (fr)	1990-04-17
AU609645B2 (en)	1991-05-02
CA2000604C (fr)	1999-07-06
KR920010873B1 (ko)	1992-12-19
JPH0793879B2 (ja)	1995-10-11
EP0364926A2 (fr)	1990-04-25
EP0364926A3 (fr)	1991-05-02
ES2061876T3 (es)	1994-12-16
DK515989D0 (da)	1989-10-17
DK515989A (da)	1990-04-18
ATE101650T1 (de)	1994-03-15

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2000-07-16	FF	Patent granted
2000-08-31	KB	Patent renewed
2003-12-10	KB	Patent renewed
2008-01-06	KB	Patent renewed
2010-05-31	EXP	Patent expired

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