JPS6474989A - Dna to code human lysozyme - Google Patents

Dna to code human lysozyme

Info

Publication number
JPS6474989A
JPS6474989A JP22975287A JP22975287A JPS6474989A JP S6474989 A JPS6474989 A JP S6474989A JP 22975287 A JP22975287 A JP 22975287A JP 22975287 A JP22975287 A JP 22975287A JP S6474989 A JPS6474989 A JP S6474989A
Authority
JP
Japan
Prior art keywords
dna
plasmid
human lysozyme
phage
code
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
JP22975287A
Other languages
Japanese (ja)
Inventor
Kazuo Nakahama
Koji Yoshimura
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.)
Takeda Pharmaceutical Co Ltd
Original Assignee
Takeda Chemical Industries Ltd
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 Takeda Chemical Industries Ltd filed Critical Takeda Chemical Industries Ltd
Priority to JP22975287A priority Critical patent/JPS6474989A/en
Publication of JPS6474989A publication Critical patent/JPS6474989A/en
Pending legal-status Critical Current

Links

Classifications

    • CCHEMISTRY; METALLURGY
    • C12BIOCHEMISTRY; BEER; SPIRITS; WINE; VINEGAR; MICROBIOLOGY; ENZYMOLOGY; MUTATION OR GENETIC ENGINEERING
    • C12NMICROORGANISMS OR ENZYMES; COMPOSITIONS THEREOF; PROPAGATING, PRESERVING, OR MAINTAINING MICROORGANISMS; MUTATION OR GENETIC ENGINEERING; CULTURE MEDIA
    • C12N9/00Enzymes; Proenzymes; Compositions thereof; Processes for preparing, activating, inhibiting, separating or purifying enzymes
    • C12N9/14Hydrolases (3)
    • C12N9/24Hydrolases (3) acting on glycosyl compounds (3.2)
    • C12N9/2402Hydrolases (3) acting on glycosyl compounds (3.2) hydrolysing O- and S- glycosyl compounds (3.2.1)
    • C12N9/2462Lysozyme (3.2.1.17)
    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K2319/00Fusion polypeptide
    • C07K2319/01Fusion polypeptide containing a localisation/targetting motif
    • C07K2319/02Fusion polypeptide containing a localisation/targetting motif containing a signal sequence

Landscapes

  • Life Sciences & Earth Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Health & Medical Sciences (AREA)
  • Genetics & Genomics (AREA)
  • Organic Chemistry (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Zoology (AREA)
  • Wood Science & Technology (AREA)
  • Molecular Biology (AREA)
  • Microbiology (AREA)
  • Biotechnology (AREA)
  • Biomedical Technology (AREA)
  • Biochemistry (AREA)
  • General Engineering & Computer Science (AREA)
  • General Health & Medical Sciences (AREA)
  • Medicinal Chemistry (AREA)
  • Enzymes And Modification Thereof (AREA)

Abstract

PURPOSE:To efficiently secrete and to manifest maturation protein of human lysozyme and to produce a large amount of the maturation protein, by cultivating a transformant transformed with DNA to code a signal peptide and the maturation protein of human lysozyme. CONSTITUTION:mRNA is separated from a human lysozyme producing cell, single stranded cDNA is synthesized from the mRNA, then double stranded DNA is synthesized, the cDNA is integrated into a phage or plasmid, a host is transformed with the phage or plasmid and the prepared transformant is cultivated and the phage or plasmid containing the aimed DNA is isolated. The aimed cloned DNA is cut out from the phage or plasmid and subcloned to a proper plasmid to give DNA to code an amino acid sequence shown by the formula. DNA to code various kinds of proteins is bonded to the 3' end of signal peptide of human lysozyme and inserted into the downstream of a promoter of a manifestation vector so that protein can be secreted and produced.
JP22975287A 1987-09-16 1987-09-16 Dna to code human lysozyme Pending JPS6474989A (en)

Priority Applications (1)

Application Number Priority Date Filing Date Title
JP22975287A JPS6474989A (en) 1987-09-16 1987-09-16 Dna to code human lysozyme

Applications Claiming Priority (1)

Application Number Priority Date Filing Date Title
JP22975287A JPS6474989A (en) 1987-09-16 1987-09-16 Dna to code human lysozyme

Publications (1)

Publication Number Publication Date
JPS6474989A true JPS6474989A (en) 1989-03-20

Family

ID=16897128

Family Applications (1)

Application Number Title Priority Date Filing Date
JP22975287A Pending JPS6474989A (en) 1987-09-16 1987-09-16 Dna to code human lysozyme

Country Status (1)

Country Link
JP (1) JPS6474989A (en)

Cited By (2)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0949692A2 (en) * 1998-03-30 1999-10-13 International Superconductivity Technology Center Oxide superconductor and method of treating the surface thereof
CN104278017A (en) * 2013-07-11 2015-01-14 上海万特医药科技有限公司 Recombinant expression method of human lysozyme

Cited By (3)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP0949692A2 (en) * 1998-03-30 1999-10-13 International Superconductivity Technology Center Oxide superconductor and method of treating the surface thereof
EP0949692A3 (en) * 1998-03-30 2004-03-31 International Superconductivity Technology Center Oxide superconductor and method of treating the surface thereof
CN104278017A (en) * 2013-07-11 2015-01-14 上海万特医药科技有限公司 Recombinant expression method of human lysozyme

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