DD301731A9 - T7 dna polymerase - Google Patents
T7 dna polymerase Download PDFInfo
- Publication number
- DD301731A9 DD301731A9 DD88332342A DD33234288A DD301731A9 DD 301731 A9 DD301731 A9 DD 301731A9 DD 88332342 A DD88332342 A DD 88332342A DD 33234288 A DD33234288 A DD 33234288A DD 301731 A9 DD301731 A9 DD 301731A9
- Authority
- DD
- German Democratic Republic
- Prior art keywords
- dna
- polymerase
- reaction
- dna polymerase
- sequencing
- Prior art date
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- 239000011737 fluorine Substances 0.000 description 1
- 229910052731 fluorine Inorganic materials 0.000 description 1
- 230000002068 genetic effect Effects 0.000 description 1
- 239000003365 glass fiber Substances 0.000 description 1
- 229910052588 hydroxylapatite Inorganic materials 0.000 description 1
- 238000000338 in vitro Methods 0.000 description 1
- 239000003112 inhibitor Substances 0.000 description 1
- 239000006166 lysate Substances 0.000 description 1
- 239000004325 lysozyme Substances 0.000 description 1
- 229960000274 lysozyme Drugs 0.000 description 1
- 235000010335 lysozyme Nutrition 0.000 description 1
- 238000013507 mapping Methods 0.000 description 1
- 238000005259 measurement Methods 0.000 description 1
- 108020004999 messenger RNA Proteins 0.000 description 1
- 239000002184 metal Substances 0.000 description 1
- 229910052751 metal Inorganic materials 0.000 description 1
- 239000006151 minimal media Substances 0.000 description 1
- 230000035772 mutation Effects 0.000 description 1
- MGFYIUFZLHCRTH-UHFFFAOYSA-N nitrilotriacetic acid Chemical compound OC(=O)CN(CC(O)=O)CC(O)=O MGFYIUFZLHCRTH-UHFFFAOYSA-N 0.000 description 1
- 150000002926 oxygen Chemical class 0.000 description 1
- XYJRXVWERLGGKC-UHFFFAOYSA-D pentacalcium;hydroxide;triphosphate Chemical compound [OH-].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[Ca+2].[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O.[O-]P([O-])([O-])=O XYJRXVWERLGGKC-UHFFFAOYSA-D 0.000 description 1
- 229940080469 phosphocellulose Drugs 0.000 description 1
- 102000020233 phosphotransferase Human genes 0.000 description 1
- 238000006116 polymerization reaction Methods 0.000 description 1
- 229920001155 polypropylene Polymers 0.000 description 1
- 238000001556 precipitation Methods 0.000 description 1
- 239000002243 precursor Substances 0.000 description 1
- 238000000163 radioactive labelling Methods 0.000 description 1
- 230000009467 reduction Effects 0.000 description 1
- 108091008146 restriction endonucleases Proteins 0.000 description 1
- 239000000523 sample Substances 0.000 description 1
- 238000002415 sodium dodecyl sulfate polyacrylamide gel electrophoresis Methods 0.000 description 1
- 238000005063 solubilization Methods 0.000 description 1
- 230000007928 solubilization Effects 0.000 description 1
- 238000003756 stirring Methods 0.000 description 1
- 239000000126 substance Substances 0.000 description 1
- 239000013589 supplement Substances 0.000 description 1
- 239000000725 suspension Substances 0.000 description 1
- 230000002194 synthesizing effect Effects 0.000 description 1
- 238000010257 thawing Methods 0.000 description 1
- RWQNBRDOKXIBIV-UHFFFAOYSA-N thymine Chemical compound CC1=CNC(=O)NC1=O RWQNBRDOKXIBIV-UHFFFAOYSA-N 0.000 description 1
- 231100000331 toxic Toxicity 0.000 description 1
- 230000002588 toxic effect Effects 0.000 description 1
- LENZDBCJOHFCAS-UHFFFAOYSA-N tris Chemical compound OCC(N)(CO)CO LENZDBCJOHFCAS-UHFFFAOYSA-N 0.000 description 1
- 239000012588 trypsin Substances 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
- C12N15/09—Recombinant DNA-technology
- C12N15/11—DNA or RNA fragments; Modified forms thereof; Non-coding nucleic acids having a biological activity
- C12N15/52—Genes encoding for enzymes or proenzymes
-
- C—CHEMISTRY; METALLURGY
- C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6869—Methods for sequencing
-
- 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
- C12N9/10—Transferases (2.)
- C12N9/12—Transferases (2.) transferring phosphorus containing groups, e.g. kinases (2.7)
- C12N9/1241—Nucleotidyltransferases (2.7.7)
- C12N9/1252—DNA-directed DNA polymerase (2.7.7.7), i.e. DNA replicase
-
- 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
- C12Q—MEASURING OR TESTING PROCESSES INVOLVING ENZYMES, NUCLEIC ACIDS OR MICROORGANISMS; COMPOSITIONS OR TEST PAPERS THEREFOR; PROCESSES OF PREPARING SUCH COMPOSITIONS; CONDITION-RESPONSIVE CONTROL IN MICROBIOLOGICAL OR ENZYMOLOGICAL PROCESSES
- C12Q1/00—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions
- C12Q1/68—Measuring or testing processes involving enzymes, nucleic acids or microorganisms; Compositions therefor; Processes of preparing such compositions involving nucleic acids
- C12Q1/6844—Nucleic acid amplification reactions
- C12Q1/686—Polymerase chain reaction [PCR]
-
- 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
- Y10S435/00—Chemistry: molecular biology and microbiology
- Y10S435/8215—Microorganisms
- Y10S435/822—Microorganisms using bacteria or actinomycetales
- Y10S435/848—Escherichia
- Y10S435/849—Escherichia coli
Landscapes
- Chemical & Material Sciences (AREA)
- Life Sciences & Earth Sciences (AREA)
- Health & Medical Sciences (AREA)
- Organic Chemistry (AREA)
- Engineering & Computer Science (AREA)
- Wood Science & Technology (AREA)
- Zoology (AREA)
- Genetics & Genomics (AREA)
- Molecular Biology (AREA)
- Bioinformatics & Cheminformatics (AREA)
- General Engineering & Computer Science (AREA)
- Biotechnology (AREA)
- Proteomics, Peptides & Aminoacids (AREA)
- Biochemistry (AREA)
- General Health & Medical Sciences (AREA)
- Microbiology (AREA)
- Chemical Kinetics & Catalysis (AREA)
- Biomedical Technology (AREA)
- Biophysics (AREA)
- Physics & Mathematics (AREA)
- Analytical Chemistry (AREA)
- Immunology (AREA)
- General Chemical & Material Sciences (AREA)
- Medicinal Chemistry (AREA)
- Plant Pathology (AREA)
- Measuring Or Testing Involving Enzymes Or Micro-Organisms (AREA)
- Saccharide Compounds (AREA)
- Enzymes And Modification Thereof (AREA)
- Investigating Or Analysing Biological Materials (AREA)
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| US07/003,227 US4795699A (en) | 1987-01-14 | 1987-01-14 | T7 DNA polymerase |
| US07/132,569 US4942130A (en) | 1987-01-14 | 1987-12-14 | T7 DNA polymerase |
| DD88312188A DD279690A5 (de) | 1987-01-14 | 1988-01-12 | Verfahren zur bestimmung der nukleotidbasenfolge eines dna molekuels |
Publications (1)
| Publication Number | Publication Date |
|---|---|
| DD301731A9 true DD301731A9 (de) | 1993-08-26 |
Family
ID=26671499
Family Applications (1)
| Application Number | Title | Priority Date | Filing Date |
|---|---|---|---|
| DD88332342A DD301731A9 (de) | 1987-01-14 | 1988-01-12 | T7 dna polymerase |
Country Status (19)
| Country | Link |
|---|---|
| US (1) | US4942130A (zh) |
| EP (5) | EP0386859B1 (zh) |
| JP (7) | JP2584644B2 (zh) |
| KR (1) | KR930005660B1 (zh) |
| CN (1) | CN1031251A (zh) |
| AT (2) | ATE118039T1 (zh) |
| AU (1) | AU604824B2 (zh) |
| CA (2) | CA1340628C (zh) |
| DD (1) | DD301731A9 (zh) |
| DE (9) | DE3751042T2 (zh) |
| DK (1) | DK13288A (zh) |
| ES (5) | ES2056366T3 (zh) |
| FI (1) | FI880131A (zh) |
| GR (2) | GR880300103T1 (zh) |
| HU (1) | HUT46069A (zh) |
| IL (1) | IL85073A (zh) |
| NO (1) | NO880126L (zh) |
| NZ (1) | NZ223039A (zh) |
| RO (1) | RO107769B1 (zh) |
Families Citing this family (41)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| JPS6384264A (ja) * | 1986-09-27 | 1988-04-14 | Toshiba Corp | 画像読取装置 |
| US4962020A (en) * | 1988-07-12 | 1990-10-09 | President And Fellows Of Harvard College | DNA sequencing |
| GB8827167D0 (en) * | 1988-11-21 | 1988-12-29 | Apothekernes Lab | In vitro mutagenesis |
| US5001050A (en) * | 1989-03-24 | 1991-03-19 | Consejo Superior Investigaciones Cientificas | PHφ29 DNA polymerase |
| US5047342A (en) * | 1989-08-10 | 1991-09-10 | Life Technologies, Inc. | Cloning and expression of T5 DNA polymerase |
| US5541099A (en) * | 1989-08-10 | 1996-07-30 | Life Technologies, Inc. | Cloning and expression of T5 DNA polymerase reduced in 3'-to-5' exonuclease activity |
| US5270179A (en) * | 1989-08-10 | 1993-12-14 | Life Technologies, Inc. | Cloning and expression of T5 DNA polymerase reduced in 3'- to-5' exonuclease activity |
| GB8926269D0 (en) * | 1989-11-21 | 1990-01-10 | Dynal As | Plasmid |
| DK0445097T3 (da) * | 1990-02-26 | 1996-09-16 | Univ Washington | Fremgangsmåde til N-myristoylering af protein |
| US5322785A (en) | 1990-04-26 | 1994-06-21 | New England Biolabs, Inc. | Purified thermostable DNA polymerase obtainable from thermococcus litoralis |
| DE69231178T2 (de) * | 1991-08-30 | 2000-11-23 | Syngenix Ltd., Cambridge | Nukleinsäure-amplifikation durch polymerase-reaktion |
| US6410277B1 (en) | 1993-02-19 | 2002-06-25 | Takara Shuzo Co., Ltd. | DNA polymersases with enhanced length of primer extension |
| US7465539B1 (en) | 1993-02-19 | 2008-12-16 | Takara Bio, Inc. | DNA polymerases with enhanced length of primer extension |
| US5436149A (en) * | 1993-02-19 | 1995-07-25 | Barnes; Wayne M. | Thermostable DNA polymerase with enhanced thermostability and enhanced length and efficiency of primer extension |
| US5547859A (en) * | 1993-08-02 | 1996-08-20 | Goodman; Myron F. | Chain-terminating nucleotides for DNA sequencing methods |
| US7312052B1 (en) | 1993-12-08 | 2007-12-25 | Stratagene California | Polymerase compositions and uses thereof |
| US6015668A (en) * | 1994-09-30 | 2000-01-18 | Life Technologies, Inc. | Cloned DNA polymerases from thermotoga and mutants thereof |
| US5614365A (en) * | 1994-10-17 | 1997-03-25 | President & Fellow Of Harvard College | DNA polymerase having modified nucleotide binding site for DNA sequencing |
| DE69400567T2 (de) * | 1994-10-17 | 1997-02-06 | President And Fellows Of Harvard College, Cambridge, Mass. | DNS Polymerase mit veränderter Nukleotid-Bindungstelle |
| AU7236296A (en) * | 1995-09-08 | 1997-03-27 | Life Technologies, Inc. | Cloned dna polymerases from thermotoga and mutants thereof |
| US5888736A (en) * | 1995-12-22 | 1999-03-30 | Visible Genetics, Inc. | Method, compositions and kit for detection and identification of microorganisms |
| US5789168A (en) * | 1996-05-01 | 1998-08-04 | Visible Genetics Inc. | Method for amplification and sequencing of nucleic acid polymers |
| US5830657A (en) * | 1996-05-01 | 1998-11-03 | Visible Genetics Inc. | Method for single-tube sequencing of nucleic acid polymers |
| US6083699A (en) * | 1996-05-01 | 2000-07-04 | Visible Genetics Inc. | Method for bi-directional sequencing of nucleic acid polymers |
| US6214555B1 (en) | 1996-05-01 | 2001-04-10 | Visible Genetics Inc. | Method compositions and kit for detection |
| US6413718B1 (en) | 1996-05-01 | 2002-07-02 | Visible Genetics Inc. | Method for sequencing of nucleic acid polymers |
| US5827716A (en) * | 1996-07-30 | 1998-10-27 | Amersham Life Science, Inc. | Modified Pol-II type DNA polymerases |
| US6291164B1 (en) | 1996-11-22 | 2001-09-18 | Invitrogen Corporation | Methods for preventing inhibition of nucleic acid synthesis by pyrophosphate |
| US5876934A (en) * | 1996-12-18 | 1999-03-02 | Pharmacia Biotech Inc. | DNA sequencing method |
| US6306588B1 (en) | 1997-02-07 | 2001-10-23 | Invitrogen Corporation | Polymerases for analyzing or typing polymorphic nucleic acid fragments and uses thereof |
| DE69838724T2 (de) | 1997-03-21 | 2008-10-30 | Stratagene California, La Jolla | Polymerase-verbessernder faktor (pef)-enthaltende extrakte, pef proteinkomplexe, isoliertes pef protein und verfahren zur reinigung und identifizierung |
| WO2000041524A2 (en) * | 1999-01-11 | 2000-07-20 | President And Fellows Of Harvard College | Isothermal amplification of dna |
| CN1313394A (zh) * | 2000-03-10 | 2001-09-19 | 上海博德基因开发有限公司 | 一种新的多肽——dna聚合酶10和编码这种多肽的多核苷酸 |
| US7198924B2 (en) | 2000-12-11 | 2007-04-03 | Invitrogen Corporation | Methods and compositions for synthesis of nucleic acid molecules using multiple recognition sites |
| US7222059B2 (en) | 2001-11-15 | 2007-05-22 | Siemens Medical Solutions Diagnostics | Electrophoretic trace simulator |
| EP1697534B1 (en) | 2003-12-01 | 2010-06-02 | Life Technologies Corporation | Nucleic acid molecules containing recombination sites and methods of using the same |
| EP2297343A1 (en) * | 2008-05-16 | 2011-03-23 | New England Biolabs, Inc. | Enzyme reagents for amplification of polynucleotides in the presence of inhibitors |
| KR101417989B1 (ko) * | 2013-02-08 | 2014-07-09 | 주식회사 엔지노믹스 | 이중가닥 dna 말단의 단일가닥 길이 조절 방법 |
| RU2020103727A (ru) | 2017-06-30 | 2021-07-30 | Кодексис, Инк. | Варианты рнк-полимеразы т7 |
| EP3645711A4 (en) | 2017-06-30 | 2021-04-21 | Codexis, Inc. | T7 RNA POLYMERASE VARIANTS |
| CN114774453B (zh) * | 2022-03-14 | 2023-04-21 | 湖北大学 | 一种运动发酵单胞菌基因表达严谨调控系统的构建方法和应用 |
Family Cites Families (33)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US3444041A (en) * | 1965-09-29 | 1969-05-13 | Univ Illinois | In vitro synthesis of ribonucleic acids and enzyme therefor |
| US3661893A (en) * | 1968-11-25 | 1972-05-09 | Univ Illinois | Synthesis in vitro of nucleic acids and products used therein and products produced therefrom |
| US4072574A (en) * | 1976-07-30 | 1978-02-07 | The Institute For Cancer Research | System for in vitro assay for mutagenicity and/or carcinogenicity of chemicals or other exogenous agents |
| US4363877B1 (en) * | 1977-09-23 | 1998-05-26 | Univ California | Recombinant dna transfer vectors |
| US4224408A (en) * | 1978-11-22 | 1980-09-23 | Abbott Laboratories | Deoxyribonucleic acid synthesis using binding protein |
| US4331589A (en) * | 1978-11-22 | 1982-05-25 | Abbott Laboratories | Deoxyribonucleic acid synthesis using binding protein extracted from chick embryo fibroblasts |
| DK145779A (da) * | 1979-04-09 | 1980-10-10 | Novo Industri As | Fremgangsmaade til termisk destabilisering af mikrobiel osteloebe |
| US4663283A (en) * | 1980-03-24 | 1987-05-05 | Genentech, Inc. | Method of altering double-stranded DNA |
| US4555486A (en) * | 1980-12-08 | 1985-11-26 | Cetus Corporation | Method for using an amino-terminus DNA sequence to synthesize a specific double-stranded DNA |
| US4394443A (en) * | 1980-12-18 | 1983-07-19 | Yale University | Method for cloning genes |
| US4395486A (en) * | 1981-08-19 | 1983-07-26 | Medical College Of Ga. Research Inst., Inc. | Method for the direct analysis of sickle cell anemia |
| FI63596C (fi) * | 1981-10-16 | 1983-07-11 | Orion Yhtymae Oy | Mikrobdiagnostiskt foerfarande som grundar sig pao skiktshybridisering av nukleinsyror och vid foerfarandet anvaenda kombinationer av reagenser |
| US4663290A (en) * | 1982-01-21 | 1987-05-05 | Molecular Genetics, Inc. | Production of reverse transcriptase |
| US4483922A (en) * | 1982-05-14 | 1984-11-20 | Amf Inc. | Inactivation of enzymes |
| US4483920A (en) * | 1982-05-17 | 1984-11-20 | Hahnemann University | Immobilization of message RNA directly from cells onto filter material |
| US4556643A (en) * | 1982-07-26 | 1985-12-03 | Agracetus | Assay method and probe for polynucleotide sequences |
| US4521509A (en) * | 1982-11-24 | 1985-06-04 | Research Corporation | Method for degrading DNA |
| GB8311018D0 (en) * | 1983-04-22 | 1983-05-25 | Amersham Int Plc | Detecting mutations in dna |
| US4729947A (en) * | 1984-03-29 | 1988-03-08 | The Board Of Regents Of The University Of Nebraska | DNA sequencing |
| US4786600A (en) * | 1984-05-25 | 1988-11-22 | The Trustees Of Columbia University In The City Of New York | Autocatalytic replication of recombinant RNA |
| US4675283A (en) * | 1984-07-19 | 1987-06-23 | Massachusetts Institute Of Technology | Detection and isolation of homologous, repeated and amplified nucleic acid sequences |
| US4767708A (en) * | 1984-08-07 | 1988-08-30 | Carnegie Mellon University | Enzyme amplification and purification |
| JPS61137158A (ja) * | 1984-12-07 | 1986-06-24 | Toshiba Corp | 電子写真感光体 |
| US4670379A (en) * | 1984-12-19 | 1987-06-02 | E. I. Du Pont De Nemours And Company | Polynucleotide hydridization assays employing catalyzed luminescence |
| US4795700A (en) * | 1985-01-25 | 1989-01-03 | California Institute Of Technology | Nucleic acid probes and methods of using same |
| JPS61219399A (ja) * | 1985-03-27 | 1986-09-29 | Hitachi Ltd | 核酸塩基配列決定法 |
| US4683195A (en) * | 1986-01-30 | 1987-07-28 | Cetus Corporation | Process for amplifying, detecting, and/or-cloning nucleic acid sequences |
| US4683202A (en) * | 1985-03-28 | 1987-07-28 | Cetus Corporation | Process for amplifying nucleic acid sequences |
| US4707235A (en) * | 1985-10-16 | 1987-11-17 | Pharmacia, Inc. | Electrophoresis method and apparatus having continuous detection means |
| JPH0732719B2 (ja) * | 1986-02-07 | 1995-04-12 | 株式会社日立製作所 | 核酸断片調製法 |
| US4800159A (en) * | 1986-02-07 | 1989-01-24 | Cetus Corporation | Process for amplifying, detecting, and/or cloning nucleic acid sequences |
| CA1338457C (en) * | 1986-08-22 | 1996-07-16 | Henry A. Erlich | Purified thermostable enzyme |
| US4795699A (en) * | 1987-01-14 | 1989-01-03 | President And Fellows Of Harvard College | T7 DNA polymerase |
-
1987
- 1987-12-14 US US07/132,569 patent/US4942130A/en not_active Expired - Lifetime
- 1987-12-22 NZ NZ223039A patent/NZ223039A/xx unknown
- 1987-12-24 DE DE3751042T patent/DE3751042T2/de not_active Expired - Lifetime
- 1987-12-24 AT AT90201140T patent/ATE118039T1/de not_active IP Right Cessation
- 1987-12-24 EP EP90201140A patent/EP0386859B1/en not_active Expired - Lifetime
- 1987-12-24 DE DE9090201138T patent/DE3781809T2/de not_active Expired - Fee Related
- 1987-12-24 DE DE199292202037T patent/DE516245T1/de active Pending
- 1987-12-24 EP EP87311435A patent/EP0265293B1/en not_active Expired - Lifetime
- 1987-12-24 DE DE3789623T patent/DE3789623T4/de not_active Expired - Lifetime
- 1987-12-24 ES ES90201138T patent/ES2056366T3/es not_active Expired - Lifetime
- 1987-12-24 ES ES92202037T patent/ES2060569T1/es active Pending
- 1987-12-24 ES ES90201139T patent/ES2063243T3/es not_active Expired - Lifetime
- 1987-12-24 AT AT87311435T patent/ATE109207T1/de not_active IP Right Cessation
- 1987-12-24 ES ES90201140T patent/ES2068323T3/es not_active Expired - Lifetime
- 1987-12-24 DE DE198787311435T patent/DE265293T1/de active Pending
- 1987-12-24 EP EP90201138A patent/EP0386857B1/en not_active Expired - Lifetime
- 1987-12-24 DE DE3750288T patent/DE3750288T2/de not_active Expired - Lifetime
- 1987-12-24 ES ES87311435T patent/ES2001837T3/es not_active Expired - Lifetime
- 1987-12-24 DE DE3789623A patent/DE3789623D1/de not_active Expired - Fee Related
- 1987-12-24 DE DE199090201140T patent/DE386859T1/de active Pending
- 1987-12-24 EP EP90201139A patent/EP0386858B1/en not_active Expired - Lifetime
- 1987-12-24 DE DE199090201139T patent/DE386858T1/de active Pending
- 1987-12-24 EP EP92202037A patent/EP0516245A1/en not_active Ceased
-
1988
- 1988-01-11 IL IL8507388A patent/IL85073A/en not_active IP Right Cessation
- 1988-01-12 DD DD88332342A patent/DD301731A9/de unknown
- 1988-01-13 CA CA000556390A patent/CA1340628C/en not_active Expired - Lifetime
- 1988-01-13 JP JP63003927A patent/JP2584644B2/ja not_active Expired - Lifetime
- 1988-01-13 CA CA000616698A patent/CA1341512C/en not_active Expired - Fee Related
- 1988-01-13 FI FI880131A patent/FI880131A/fi not_active Application Discontinuation
- 1988-01-13 HU HU88128A patent/HUT46069A/hu unknown
- 1988-01-13 NO NO880126A patent/NO880126L/no unknown
- 1988-01-13 DK DK013288A patent/DK13288A/da not_active Application Discontinuation
- 1988-01-13 RO RO131762A patent/RO107769B1/ro unknown
- 1988-01-13 AU AU10224/88A patent/AU604824B2/en not_active Ceased
- 1988-01-14 CN CN88100646A patent/CN1031251A/zh active Pending
- 1988-01-14 KR KR1019880000286A patent/KR930005660B1/ko not_active IP Right Cessation
- 1988-10-21 GR GR88300103T patent/GR880300103T1/el unknown
-
1992
- 1992-11-19 JP JP4333525A patent/JPH0670772A/ja active Pending
- 1992-11-19 JP JP4333524A patent/JPH06237765A/ja active Pending
- 1992-11-19 JP JP4333528A patent/JP2606777B2/ja not_active Expired - Lifetime
- 1992-11-19 JP JP4333527A patent/JPH0746990A/ja active Pending
- 1992-11-19 JP JP4333526A patent/JPH0670773A/ja active Pending
- 1992-12-02 GR GR920402806T patent/GR3006442T3/el unknown
-
1993
- 1993-05-18 JP JP5138959A patent/JPH06141898A/ja active Pending
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