JPS6434286A - Production of luciferase - Google Patents

Production of luciferase

Info

Publication number
JPS6434286A
JPS6434286A JP18772487A JP18772487A JPS6434286A JP S6434286 A JPS6434286 A JP S6434286A JP 18772487 A JP18772487 A JP 18772487A JP 18772487 A JP18772487 A JP 18772487A JP S6434286 A JPS6434286 A JP S6434286A
Authority
JP
Japan
Prior art keywords
afford
dna
luciferase
luc
culture medium
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.)
Pending
Application number
JP18772487A
Other languages
Japanese (ja)
Inventor
Tsutomu Masuda
Hiroki Tatsumi
Eiichi Nakano
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Kikkoman Corp
Original Assignee
Kikkoman Corp
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.)
Filing date
Publication date
Application filed by Kikkoman Corp filed Critical Kikkoman Corp
Priority to JP18772487A priority Critical patent/JPS6434286A/en
Priority to US07/224,445 priority patent/US4968613A/en
Priority to DE3887223T priority patent/DE3887223T2/en
Priority to EP88112233A priority patent/EP0301541B1/en
Publication of JPS6434286A publication Critical patent/JPS6434286A/en
Pending legal-status Critical Current

Links

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
    • C12N9/0004—Oxidoreductases (1.)
    • C12N9/0069—Oxidoreductases (1.) acting on single donors with incorporation of molecular oxygen, i.e. oxygenases (1.13)
    • C—CHEMISTRY; METALLURGY
    • C12—BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12Y—ENZYMES
    • C12Y113/00—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13)
    • C12Y113/12—Oxidoreductases acting on single donors with incorporation of molecular oxygen (oxygenases) (1.13) with incorporation of one atom of oxygen (internal monooxygenases or internal mixed function oxidases)(1.13.12)
    • C12Y113/12007—Photinus-luciferin 4-monooxygenase (ATP-hydrolysing) (1.13.12.7), i.e. firefly-luciferase

Abstract

PURPOSE:To efficiently obtain luciferase useful as an enzyme for determining adenosine triphosphate (ATP), etc., in a short time, by cultivating a specific microorganism in a culture medium. CONSTITUTION:A DNA capable of coding luciferase (LUC) derived from a Photinus.pyralis which is a species of firefly and c-DNA derived from Luciola.cruciata which is 'GENJI BOTARU' are hybridized to provide a plasmid DNA (A) containing the c-DNA capable of coding LUC of about 2.0 kb. The resultant component (A) is then treated with a restriction enzyme to afford a DNA, which is subsequently integrated into a plasmid pUC18 to afford a recombinant DAN (B). The obtained component (B) is then introduced into Escherichia coli JM101 of the genus Escherichia, etc., to provide a microorganism (C) having the ability to produce LUC. The resultant strain (C) is subsequently cultivated in a culture medium containing trypton, etc., at 30-40 deg.C for 4-8hr and centrifuged to afford microbial cells, which are crushed to provide a crude enzyme liquid (D). The obtained liquid (D) is then subjected to purification treatment, such as fractionation with sodium sulfate or gel filtration, to afford the aimed purified luciferase.
JP18772487A 1987-07-29 1987-07-29 Production of luciferase Pending JPS6434286A (en)

Priority Applications (4)

Application Number Priority Date Filing Date Title
JP18772487A JPS6434286A (en) 1987-07-29 1987-07-29 Production of luciferase
US07/224,445 US4968613A (en) 1987-07-29 1988-07-26 Luciferase gene and novel recombinant DNA as well as a method of producing luciferase
DE3887223T DE3887223T2 (en) 1987-07-29 1988-07-28 Luciferase gene and new recombinant DNA and a process for the production of luciferase.
EP88112233A EP0301541B1 (en) 1987-07-29 1988-07-28 Luciferase gene and novel recombinant DNA as well as a method of producing luciferase

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP18772487A JPS6434286A (en) 1987-07-29 1987-07-29 Production of luciferase

Publications (1)

Publication Number Publication Date
JPS6434286A true JPS6434286A (en) 1989-02-03

Family

ID=16211070

Family Applications (1)

Application Number Title Priority Date Filing Date
JP18772487A Pending JPS6434286A (en) 1987-07-29 1987-07-29 Production of luciferase

Country Status (1)

Country Link
JP (1) JPS6434286A (en)

Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6143998A (en) * 1984-06-05 1986-03-03 アマーシャム　インターナショナル　パブリック　リミティド　カンパニー Detection of bacteria in environment

Patent Citations (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPS6143998A (en) * 1984-06-05 1986-03-03 アマーシャム　インターナショナル　パブリック　リミティド　カンパニー Detection of bacteria in environment

Similar Documents

Publication Publication Date Title
AR001934A1 (en) Bioconversion process to produce 1,3-propanediol
CN100413967C (en) (R)-2-octanol dehydrogenase, process for producing enzyme, DNA encoding enzyme and process for producing alcohol by using same
Ueno et al. Purification and characterization of hydrogenase from the marine green alga, Chlorococcum littorale
EP0625571A3 (en) Microorganisms, their use and method of production of L-alpha-amino acids.
SCHÄR et al. Purification and characterization of N, N‐dimethylformamidase from Pseudomonas DMF 3/3
Ueda et al. Purification and characterization of two types of fumarase from Escherichia coli
MC2145A1 (en) PROTEIN HAVING URATE OXIDASE ACTIVITY, RECOMBINANT GENE ENCODING THE SAME, EXPRESSION VECTOR, MICROORGANISMS AND TRANSFORMED CELLS
DE68926893T2 (en) Process for the production of clavulanic acid
Kaziro et al. Crystalline G factor from Escherichia coli
AU667706B2 (en) Endo-xyloglucan transferase
Yamanaka et al. Purification and properties of cytochrome c-553 and cytochrome B-560 from Tetrahymena pyriformis
Ngai et al. Abundant expression of Pseudomonas genes for chlorocatechol metabolism
JPS6434286A (en) Production of luciferase
Viswanath-Reddy et al. Purification and properties of NADP+-linked glycerol dehydrogenase from Neurospora crassa
Schneider et al. Phytoene desaturase: heterologous expression in an active state, purification, and biochemical properties
Massadeh et al. Purification of lipase enzyme produced by Bacillus stearothermophilus HU1
Chowdhury et al. 3-Hydroxyisobutyrate dehydrogenase from Pseudomonas putida E23: purification and characterization
Natake Studies on Glucose-Isomerizing Enzyme of Bacteria: Part IV. Purification and Properties of the Enzyme from Escherichia intermedia, Strain HN-500
Maruyama Purification and properties of γ-oxalomesaconate hydratase from Pseudomonas ochraceae grown with phthalate
IMANAGA METABOLISM OF D-GLUCOSAMINE III. ENZYMIC DEGRADATION OF D-GLUCOSAMINIC ACID
Petushkov et al. Purification and partial spectral characterization of a novel luciferin from the luminous enchytraeid Fridericia heliota
Gleason et al. Lactic acid fermentation in lower fungi
JP3029915B2 (en) Thermostable adenosine-5'-phosphosulfate kinase and method for producing the same
EA200200056A1 (en) STREPTOMYCES AVERMITILIS GENE, GUIDES TO B2: B1 RELATIONSHIP
Suzuki et al. Inhibition of DNA topoisomerases by microbial inhibitors