CH637991A5 - Verfahren zur herstellung einer leichten (b) plasmin-kettenfraktion mit einem aktiven serinproteasezentrum. - Google Patents
Verfahren zur herstellung einer leichten (b) plasmin-kettenfraktion mit einem aktiven serinproteasezentrum. Download PDFInfo
- Publication number
- CH637991A5 CH637991A5 CH1165677A CH1165677A CH637991A5 CH 637991 A5 CH637991 A5 CH 637991A5 CH 1165677 A CH1165677 A CH 1165677A CH 1165677 A CH1165677 A CH 1165677A CH 637991 A5 CH637991 A5 CH 637991A5
- Authority
- CH
- Switzerland
- Prior art keywords
- light
- plasmin
- chain fraction
- streptokinase
- chain
- Prior art date
Links
- 102000012479 Serine Proteases Human genes 0.000 title claims description 22
- 238000004519 manufacturing process Methods 0.000 title description 3
- 229940012957 plasmin Drugs 0.000 claims description 107
- 229960005202 streptokinase Drugs 0.000 claims description 88
- 108010023197 Streptokinase Proteins 0.000 claims description 71
- 102000013566 Plasminogen Human genes 0.000 claims description 31
- 108010051456 Plasminogen Proteins 0.000 claims description 31
- 239000000203 mixture Substances 0.000 claims description 16
- DGVVWUTYPXICAM-UHFFFAOYSA-N β‐Mercaptoethanol Chemical compound OCCS DGVVWUTYPXICAM-UHFFFAOYSA-N 0.000 claims description 12
- 239000003112 inhibitor Substances 0.000 claims description 11
- 238000000034 method Methods 0.000 claims description 8
- 229920002684 Sepharose Polymers 0.000 claims description 7
- 238000002360 preparation method Methods 0.000 claims description 6
- 230000002441 reversible effect Effects 0.000 claims description 6
- AGDSCTQQXMDDCV-UHFFFAOYSA-M sodium;2-iodoacetate Chemical compound [Na+].[O-]C(=O)CI AGDSCTQQXMDDCV-UHFFFAOYSA-M 0.000 claims description 6
- 239000004472 Lysine Substances 0.000 claims description 5
- KDXKERNSBIXSRK-YFKPBYRVSA-N L-Lysine Natural products NCCCC[C@H](N)C(O)=O KDXKERNSBIXSRK-YFKPBYRVSA-N 0.000 claims description 4
- 230000008569 process Effects 0.000 claims description 4
- 238000000926 separation method Methods 0.000 claims description 4
- 235000019766 L-Lysine Nutrition 0.000 claims description 3
- 125000001176 L-lysyl group Chemical group [H]N([H])[C@]([H])(C(=O)[*])C([H])([H])C([H])([H])C([H])([H])C(N([H])[H])([H])[H] 0.000 claims description 2
- 238000010828 elution Methods 0.000 claims description 2
- 239000007795 chemical reaction product Substances 0.000 claims 2
- 108010088842 Fibrinolysin Proteins 0.000 description 98
- 235000018102 proteins Nutrition 0.000 description 54
- 108090000623 proteins and genes Proteins 0.000 description 54
- 102000004169 proteins and genes Human genes 0.000 description 54
- 230000000694 effects Effects 0.000 description 36
- 101000605403 Homo sapiens Plasminogen Proteins 0.000 description 16
- 102000001938 Plasminogen Activators Human genes 0.000 description 16
- 229940127126 plasminogen activator Drugs 0.000 description 16
- 230000002797 proteolythic effect Effects 0.000 description 15
- GDBQQVLCIARPGH-UHFFFAOYSA-N Leupeptin Natural products CC(C)CC(NC(C)=O)C(=O)NC(CC(C)C)C(=O)NC(C=O)CCCN=C(N)N GDBQQVLCIARPGH-UHFFFAOYSA-N 0.000 description 12
- FAPWRFPIFSIZLT-UHFFFAOYSA-M Sodium chloride Chemical compound [Na+].[Cl-] FAPWRFPIFSIZLT-UHFFFAOYSA-M 0.000 description 12
- BECPQYXYKAMYBN-UHFFFAOYSA-N casein, tech. Chemical compound NCCCCC(C(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(CC(C)C)N=C(O)C(CCC(O)=O)N=C(O)C(CC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(C(C)O)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=N)N=C(O)C(CCC(O)=O)N=C(O)C(CCC(O)=O)N=C(O)C(COP(O)(O)=O)N=C(O)C(CCC(O)=N)N=C(O)C(N)CC1=CC=CC=C1 BECPQYXYKAMYBN-UHFFFAOYSA-N 0.000 description 12
- GDBQQVLCIARPGH-ULQDDVLXSA-N leupeptin Chemical compound CC(C)C[C@H](NC(C)=O)C(=O)N[C@@H](CC(C)C)C(=O)N[C@H](C=O)CCCN=C(N)N GDBQQVLCIARPGH-ULQDDVLXSA-N 0.000 description 12
- 108010052968 leupeptin Proteins 0.000 description 12
- 239000005018 casein Substances 0.000 description 11
- 235000021240 caseins Nutrition 0.000 description 11
- 239000000758 substrate Substances 0.000 description 11
- 101001067249 Bos taurus Plasminogen Proteins 0.000 description 10
- 239000000463 material Substances 0.000 description 10
- 208000007536 Thrombosis Diseases 0.000 description 8
- 238000010438 heat treatment Methods 0.000 description 7
- 239000000243 solution Substances 0.000 description 7
- PEDCQBHIVMGVHV-UHFFFAOYSA-N Glycerine Chemical compound OCC(O)CO PEDCQBHIVMGVHV-UHFFFAOYSA-N 0.000 description 6
- 108010022999 Serine Proteases Proteins 0.000 description 6
- 238000006243 chemical reaction Methods 0.000 description 6
- 239000000047 product Substances 0.000 description 6
- 239000000872 buffer Substances 0.000 description 5
- 230000001698 pyrogenic effect Effects 0.000 description 5
- 239000007858 starting material Substances 0.000 description 5
- XLYOFNOQVPJJNP-UHFFFAOYSA-N water Substances O XLYOFNOQVPJJNP-UHFFFAOYSA-N 0.000 description 5
- BFNBIHQBYMNNAN-UHFFFAOYSA-N ammonium sulfate Chemical compound N.N.OS(O)(=O)=O BFNBIHQBYMNNAN-UHFFFAOYSA-N 0.000 description 4
- 229910052921 ammonium sulfate Inorganic materials 0.000 description 4
- 235000011130 ammonium sulphate Nutrition 0.000 description 4
- 230000000890 antigenic effect Effects 0.000 description 4
- 239000008280 blood Substances 0.000 description 4
- 210000004369 blood Anatomy 0.000 description 4
- 230000003197 catalytic effect Effects 0.000 description 4
- 239000000356 contaminant Substances 0.000 description 4
- 230000003480 fibrinolytic effect Effects 0.000 description 4
- 239000002244 precipitate Substances 0.000 description 4
- 238000006722 reduction reaction Methods 0.000 description 4
- 239000011780 sodium chloride Substances 0.000 description 4
- 238000001179 sorption measurement Methods 0.000 description 4
- 230000003612 virological effect Effects 0.000 description 4
- 241000282326 Felis catus Species 0.000 description 3
- 102000009123 Fibrin Human genes 0.000 description 3
- 108010073385 Fibrin Proteins 0.000 description 3
- BWGVNKXGVNDBDI-UHFFFAOYSA-N Fibrin monomer Chemical compound CNC(=O)CNC(=O)CN BWGVNKXGVNDBDI-UHFFFAOYSA-N 0.000 description 3
- 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
- 239000002168 alkylating agent Substances 0.000 description 3
- 229940100198 alkylating agent Drugs 0.000 description 3
- 239000012062 aqueous buffer Substances 0.000 description 3
- PXXJHWLDUBFPOL-UHFFFAOYSA-N benzamidine Chemical compound NC(=N)C1=CC=CC=C1 PXXJHWLDUBFPOL-UHFFFAOYSA-N 0.000 description 3
- 238000005119 centrifugation Methods 0.000 description 3
- MUCZHBLJLSDCSD-UHFFFAOYSA-N diisopropyl fluorophosphate Chemical compound CC(C)OP(F)(=O)OC(C)C MUCZHBLJLSDCSD-UHFFFAOYSA-N 0.000 description 3
- 229950003499 fibrin Drugs 0.000 description 3
- 239000008103 glucose Substances 0.000 description 3
- 239000007791 liquid phase Substances 0.000 description 3
- 229920002401 polyacrylamide Polymers 0.000 description 3
- 230000009467 reduction Effects 0.000 description 3
- 125000003396 thiol group Chemical group [H]S* 0.000 description 3
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 3
- 229920000936 Agarose Polymers 0.000 description 2
- 102000009027 Albumins Human genes 0.000 description 2
- 108010088751 Albumins Proteins 0.000 description 2
- 102000008100 Human Serum Albumin Human genes 0.000 description 2
- 108091006905 Human Serum Albumin Proteins 0.000 description 2
- KDXKERNSBIXSRK-UHFFFAOYSA-N Lysine Natural products NCCCCC(N)C(O)=O KDXKERNSBIXSRK-UHFFFAOYSA-N 0.000 description 2
- 239000007983 Tris buffer Substances 0.000 description 2
- 241000700605 Viruses Species 0.000 description 2
- 230000009471 action Effects 0.000 description 2
- 239000012190 activator Substances 0.000 description 2
- 239000003463 adsorbent Substances 0.000 description 2
- 238000005804 alkylation reaction Methods 0.000 description 2
- 239000003054 catalyst Substances 0.000 description 2
- 239000003638 chemical reducing agent Substances 0.000 description 2
- VHJLVAABSRFDPM-ZXZARUISSA-N dithioerythritol Chemical compound SC[C@H](O)[C@H](O)CS VHJLVAABSRFDPM-ZXZARUISSA-N 0.000 description 2
- 239000003814 drug Substances 0.000 description 2
- 239000003527 fibrinolytic agent Substances 0.000 description 2
- 230000005764 inhibitory process Effects 0.000 description 2
- 235000018977 lysine Nutrition 0.000 description 2
- 239000012064 sodium phosphate buffer Substances 0.000 description 2
- 108010008962 streptokinase-plasminogen complex Proteins 0.000 description 2
- 230000001225 therapeutic effect Effects 0.000 description 2
- SLXKOJJOQWFEFD-UHFFFAOYSA-N 6-aminohexanoic acid Chemical compound NCCCCCC(O)=O SLXKOJJOQWFEFD-UHFFFAOYSA-N 0.000 description 1
- 102000004506 Blood Proteins Human genes 0.000 description 1
- 108010017384 Blood Proteins Proteins 0.000 description 1
- 241000283690 Bos taurus Species 0.000 description 1
- KDXKERNSBIXSRK-RXMQYKEDSA-N D-lysine group Chemical group N[C@H](CCCCN)C(=O)O KDXKERNSBIXSRK-RXMQYKEDSA-N 0.000 description 1
- 102000010911 Enzyme Precursors Human genes 0.000 description 1
- 108010062466 Enzyme Precursors Proteins 0.000 description 1
- 108090000790 Enzymes Proteins 0.000 description 1
- 102000004190 Enzymes Human genes 0.000 description 1
- ODKSFYDXXFIFQN-BYPYZUCNSA-N L-arginine Chemical compound OC(=O)[C@@H](N)CCCN=C(N)N ODKSFYDXXFIFQN-BYPYZUCNSA-N 0.000 description 1
- 229930064664 L-arginine Natural products 0.000 description 1
- 235000014852 L-arginine Nutrition 0.000 description 1
- 108091005804 Peptidases Proteins 0.000 description 1
- 102000035195 Peptidases Human genes 0.000 description 1
- 206010034719 Personality change Diseases 0.000 description 1
- 108010001014 Plasminogen Activators Proteins 0.000 description 1
- 241000194017 Streptococcus Species 0.000 description 1
- 238000002835 absorbance Methods 0.000 description 1
- 238000011481 absorbance measurement Methods 0.000 description 1
- 230000002411 adverse Effects 0.000 description 1
- 230000029936 alkylation Effects 0.000 description 1
- 238000003453 ammonium sulfate precipitation method Methods 0.000 description 1
- 239000000427 antigen Substances 0.000 description 1
- 102000036639 antigens Human genes 0.000 description 1
- 108091007433 antigens Proteins 0.000 description 1
- 238000010923 batch production Methods 0.000 description 1
- 230000015572 biosynthetic process Effects 0.000 description 1
- 230000037396 body weight Effects 0.000 description 1
- 239000007853 buffer solution Substances 0.000 description 1
- 230000008859 change Effects 0.000 description 1
- 238000013375 chromatographic separation Methods 0.000 description 1
- 238000004140 cleaning Methods 0.000 description 1
- 238000005345 coagulation Methods 0.000 description 1
- 230000015271 coagulation Effects 0.000 description 1
- 230000000295 complement effect Effects 0.000 description 1
- 238000010668 complexation reaction Methods 0.000 description 1
- 239000012141 concentrate Substances 0.000 description 1
- 238000005859 coupling reaction Methods 0.000 description 1
- 230000009849 deactivation Effects 0.000 description 1
- 238000000502 dialysis Methods 0.000 description 1
- VHJLVAABSRFDPM-QWWZWVQMSA-N dithiothreitol Chemical compound SC[C@@H](O)[C@H](O)CS VHJLVAABSRFDPM-QWWZWVQMSA-N 0.000 description 1
- 229940079593 drug Drugs 0.000 description 1
- 229940088598 enzyme Drugs 0.000 description 1
- 235000013305 food Nutrition 0.000 description 1
- 230000036541 health Effects 0.000 description 1
- 208000006454 hepatitis Diseases 0.000 description 1
- 231100000283 hepatitis Toxicity 0.000 description 1
- 239000012535 impurity Substances 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 238000002347 injection Methods 0.000 description 1
- 239000007924 injection Substances 0.000 description 1
- 238000001990 intravenous administration Methods 0.000 description 1
- PGLTVOMIXTUURA-UHFFFAOYSA-N iodoacetamide Chemical compound NC(=O)CI PGLTVOMIXTUURA-UHFFFAOYSA-N 0.000 description 1
- 239000007788 liquid Substances 0.000 description 1
- 210000004072 lung Anatomy 0.000 description 1
- 238000002156 mixing Methods 0.000 description 1
- 230000008520 organization Effects 0.000 description 1
- 230000035515 penetration Effects 0.000 description 1
- 231100000572 poisoning Toxicity 0.000 description 1
- 230000000607 poisoning effect Effects 0.000 description 1
- 239000000843 powder Substances 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 125000006239 protecting group Chemical group 0.000 description 1
- 235000004252 protein component Nutrition 0.000 description 1
- 239000012460 protein solution Substances 0.000 description 1
- 230000004044 response Effects 0.000 description 1
- 230000009291 secondary effect Effects 0.000 description 1
- 239000007787 solid Substances 0.000 description 1
- 230000000087 stabilizing effect Effects 0.000 description 1
- 229960000103 thrombolytic agent Drugs 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
- 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)
- C12N9/6435—Plasmin (3.4.21.7), i.e. fibrinolysin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61P—SPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
- A61P7/00—Drugs for disorders of the blood or the extracellular fluid
- A61P7/02—Antithrombotic agents; Anticoagulants; Platelet aggregation inhibitors
-
- 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)
- C12Y304/21007—Plasmin (3.4.21.7), i.e. fibrinolysin
-
- A—HUMAN NECESSITIES
- A61—MEDICAL OR VETERINARY SCIENCE; HYGIENE
- A61K—PREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
- A61K38/00—Medicinal preparations containing peptides
Landscapes
- Health & Medical Sciences (AREA)
- Chemical & Material Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Life Sciences & Earth Sciences (AREA)
- Bioinformatics & Cheminformatics (AREA)
- Zoology (AREA)
- Wood Science & Technology (AREA)
- Genetics & Genomics (AREA)
- General Health & Medical Sciences (AREA)
- Biomedical Technology (AREA)
- Biochemistry (AREA)
- General Engineering & Computer Science (AREA)
- Medicinal Chemistry (AREA)
- Microbiology (AREA)
- Biotechnology (AREA)
- Molecular Biology (AREA)
- Public Health (AREA)
- Pharmacology & Pharmacy (AREA)
- Hematology (AREA)
- Animal Behavior & Ethology (AREA)
- Diabetes (AREA)
- Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
- Veterinary Medicine (AREA)
- General Chemical & Material Sciences (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)
- Enzymes And Modification Thereof (AREA)
- Medicines Containing Material From Animals Or Micro-Organisms (AREA)
Applications Claiming Priority (1)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US05/726,142 US4082612A (en) | 1976-09-24 | 1976-09-24 | Plasminogen activator complex |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| CH637991A5 true CH637991A5 (de) | 1983-08-31 |
Family
ID=24917422
Family Applications (2)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CH1165677A CH637991A5 (de) | 1976-09-24 | 1977-09-23 | Verfahren zur herstellung einer leichten (b) plasmin-kettenfraktion mit einem aktiven serinproteasezentrum. |
| CH511282A CH637992A5 (de) | 1976-09-24 | 1982-08-27 | Verfahren zur herstellung eines komplexes aus streptokinase und einer leichten (b) plasmin-kettenfraktion mit einem aktiven serinprotease-zentrum. |
Family Applications After (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| CH511282A CH637992A5 (de) | 1976-09-24 | 1982-08-27 | Verfahren zur herstellung eines komplexes aus streptokinase und einer leichten (b) plasmin-kettenfraktion mit einem aktiven serinprotease-zentrum. |
Country Status (10)
| Country | Link |
|---|---|
| US (1) | US4082612A (enExample) |
| JP (1) | JPS5352606A (enExample) |
| CA (1) | CA1094449A (enExample) |
| CH (2) | CH637991A5 (enExample) |
| DE (1) | DE2742529C2 (enExample) |
| DK (1) | DK421577A (enExample) |
| FR (1) | FR2365583A1 (enExample) |
| GB (1) | GB1533205A (enExample) |
| NL (1) | NL7710451A (enExample) |
| SE (3) | SE442304B (enExample) |
Families Citing this family (17)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| EP0028489B1 (en) * | 1979-11-05 | 1983-10-05 | Beecham Group Plc | Enzyme derivatives, and their preparation |
| JPS58189122A (ja) * | 1982-04-30 | 1983-11-04 | Kaken Pharmaceut Co Ltd | 高脂血症予防治療剤 |
| EP0109653A3 (en) * | 1982-11-17 | 1986-01-29 | Otsuka Pharmaceutical Co., Ltd. | Process for preparing urokinase complex |
| JPS60136520A (ja) * | 1983-12-23 | 1985-07-20 | Otsuka Pharmaceut Co Ltd | フイブリン吸着性ウロキナ−ゼ複合体 |
| GB8334498D0 (en) * | 1983-12-24 | 1984-02-01 | Beecham Group Plc | Compounds |
| GB8334499D0 (en) * | 1983-12-24 | 1984-02-01 | Beecham Group Plc | Derivatives |
| US4880776A (en) * | 1983-12-24 | 1989-11-14 | Beecham Group P.L.C. | Plasmin A-chain urokinase B-chain hybrid protein |
| GB8400653D0 (en) * | 1984-01-11 | 1984-02-15 | Beecham Group Plc | Conjugates |
| EP0156169B1 (en) * | 1984-02-29 | 1991-12-18 | Asahi Kasei Kogyo Kabushiki Kaisha | An aqueous solution of a tissue plasminogen activator dissolved therein at an increased concentration and a method |
| US4774087A (en) * | 1987-08-14 | 1988-09-27 | Northwestern University | Micro-size fibrinolytic plasmin |
| DE3833936C1 (enExample) * | 1988-10-05 | 1989-09-21 | Henning Berlin Gmbh Chemie- Und Pharmawerk, 1000 Berlin, De | |
| US6355243B1 (en) | 1999-11-13 | 2002-03-12 | Bayer Corporation | Method of thrombolysis by local delivery of active plasmin |
| US6964764B2 (en) * | 1999-11-13 | 2005-11-15 | Talecris Biotherapeutics, Inc. | Method of thrombolysis by local delivery of reversibly inactivated acidified plasmin |
| US7544500B2 (en) * | 1999-11-13 | 2009-06-09 | Talecris Biotherapeutics, Inc. | Process for the production of a reversibly inactive acidified plasmin composition |
| US6969515B2 (en) | 1999-11-13 | 2005-11-29 | Talecris Biotherapeutics, Inc. | Method of thrombolysis by local delivery of reversibly inactivated acidified plasmin |
| NZ589557A (en) * | 2008-06-04 | 2012-08-31 | Talecris Biotherapeutics Inc | Immobilised streptokinase, method and kit for preparing plasmin |
| HUE025670T2 (en) | 2009-03-03 | 2016-04-28 | Grifols Therapeutics Inc | A method for producing plasminogen |
Family Cites Families (1)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3865692A (en) * | 1974-01-11 | 1975-02-11 | Abbott Lab | Method for making highly potent plasminogen |
-
1976
- 1976-09-24 US US05/726,142 patent/US4082612A/en not_active Expired - Lifetime
-
1977
- 1977-08-16 CA CA284,760A patent/CA1094449A/en not_active Expired
- 1977-09-19 GB GB38933/77A patent/GB1533205A/en not_active Expired
- 1977-09-21 JP JP11276977A patent/JPS5352606A/ja active Pending
- 1977-09-21 DE DE2742529A patent/DE2742529C2/de not_active Expired
- 1977-09-22 FR FR7728611A patent/FR2365583A1/fr active Granted
- 1977-09-22 SE SE7710653A patent/SE442304B/xx not_active IP Right Cessation
- 1977-09-23 NL NL7710451A patent/NL7710451A/xx not_active Application Discontinuation
- 1977-09-23 CH CH1165677A patent/CH637991A5/de not_active IP Right Cessation
- 1977-09-23 DK DK421577A patent/DK421577A/da not_active Application Discontinuation
-
1982
- 1982-08-27 CH CH511282A patent/CH637992A5/de not_active IP Right Cessation
-
1983
- 1983-03-30 SE SE8301795A patent/SE454048B/sv not_active IP Right Cessation
- 1983-03-30 SE SE8301794A patent/SE454047B/sv not_active IP Right Cessation
Also Published As
| Publication number | Publication date |
|---|---|
| FR2365583A1 (fr) | 1978-04-21 |
| FR2365583B1 (enExample) | 1981-07-10 |
| SE8301795D0 (sv) | 1983-03-30 |
| SE454048B (sv) | 1988-03-28 |
| SE454047B (sv) | 1988-03-28 |
| DE2742529C2 (de) | 1984-01-05 |
| SE8301795L (sv) | 1983-03-30 |
| US4082612A (en) | 1978-04-04 |
| SE442304B (sv) | 1985-12-16 |
| DE2742529A1 (de) | 1978-03-30 |
| CH637992A5 (de) | 1983-08-31 |
| GB1533205A (en) | 1978-11-22 |
| SE7710653L (sv) | 1978-03-25 |
| DK421577A (da) | 1978-03-25 |
| JPS5352606A (en) | 1978-05-13 |
| NL7710451A (nl) | 1978-03-29 |
| CA1094449A (en) | 1981-01-27 |
| SE8301794D0 (sv) | 1983-03-30 |
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