IL85073A - A method for determining the nucleotide base sequence of a DNA molecule that uses a DNA polymerase that is processed and set for it - Google Patents
A method for determining the nucleotide base sequence of a DNA molecule that uses a DNA polymerase that is processed and set for itInfo
- Publication number
- IL85073A IL85073A IL8507388A IL8507388A IL85073A IL 85073 A IL85073 A IL 85073A IL 8507388 A IL8507388 A IL 8507388A IL 8507388 A IL8507388 A IL 8507388A IL 85073 A IL85073 A IL 85073A
- Authority
- IL
- Israel
- Prior art keywords
- polymerase
- dna
- exonuclease activity
- molecule
- nucleotide base
- Prior art date
Links
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- 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
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- 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
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- 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)
Priority Applications (5)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
IL10106188A IL101061A (en) | 1987-01-14 | 1988-01-11 | Genes encoding T7 dna polymerase |
IL10106088A IL101060A (en) | 1987-01-14 | 1988-01-11 | Composition comprising modified T7 dna polymerase and preparation thereof |
IL101061A IL101061A0 (en) | 1987-01-14 | 1992-02-24 | T7 dna polymerase |
IL101060A IL101060A0 (en) | 1987-01-14 | 1992-02-24 | T7 dna polymerase |
IL106235A IL106235A0 (en) | 1987-01-14 | 1993-07-05 | A method for determining the nucleotide base sequence of a dna molecule |
Applications Claiming Priority (2)
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 |
Publications (2)
Publication Number | Publication Date |
---|---|
IL85073A0 IL85073A0 (en) | 1988-06-30 |
IL85073A true IL85073A (en) | 1994-10-07 |
Family
ID=26671499
Family Applications (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
IL8507388A IL85073A (en) | 1987-01-14 | 1988-01-11 | A method for determining the nucleotide base sequence of a DNA molecule that uses a DNA polymerase that is processed and set for it |
Country Status (19)
Country | Link |
---|---|
US (1) | US4942130A (fr) |
EP (5) | EP0386859B1 (fr) |
JP (7) | JP2584644B2 (fr) |
KR (1) | KR930005660B1 (fr) |
CN (1) | CN1031251A (fr) |
AT (2) | ATE118039T1 (fr) |
AU (1) | AU604824B2 (fr) |
CA (2) | CA1340628C (fr) |
DD (1) | DD301731A9 (fr) |
DE (9) | DE3751042T2 (fr) |
DK (1) | DK13288A (fr) |
ES (5) | ES2056366T3 (fr) |
FI (1) | FI880131A (fr) |
GR (2) | GR880300103T1 (fr) |
HU (1) | HUT46069A (fr) |
IL (1) | IL85073A (fr) |
NO (1) | NO880126L (fr) |
NZ (1) | NZ223039A (fr) |
RO (1) | RO107769B1 (fr) |
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 (fr) * | 1999-01-11 | 2000-07-20 | President And Fellows Of Harvard College | Amplification isotherme d'adn |
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 (fr) | 2003-12-01 | 2010-06-02 | Life Technologies Corporation | Molecule d'acide nucleique contenant des sites de recombinaison et leurs procedes d'utilisation |
EP2297343A1 (fr) * | 2008-05-16 | 2011-03-23 | New England Biolabs, Inc. | Réactifs enzymatiques pour l'amplification de polynucléotides en présence d'inhibiteurs |
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 (fr) | 2017-06-30 | 2021-04-21 | Codexis, Inc. | Variants d'arn polymérase t7 |
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 (fr) * | 1986-08-22 | 1996-07-16 | Henry A. Erlich | Enzyme thermostable purifiee |
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/fr 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/fr 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/fr 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/fr not_active Expired - Lifetime
- 1987-12-24 DE DE199090201139T patent/DE386858T1/de active Pending
- 1987-12-24 EP EP92202037A patent/EP0516245A1/fr 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/fr not_active Expired - Lifetime
- 1988-01-13 JP JP63003927A patent/JP2584644B2/ja not_active Expired - Lifetime
- 1988-01-13 CA CA000616698A patent/CA1341512C/fr 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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