WO2009057622A1 - Method for production of human growth hormone improved in efficiency - Google Patents

Method for production of human growth hormone improved in efficiency Download PDF

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Publication number
WO2009057622A1
WO2009057622A1 PCT/JP2008/069616 JP2008069616W WO2009057622A1 WO 2009057622 A1 WO2009057622 A1 WO 2009057622A1 JP 2008069616 W JP2008069616 W JP 2008069616W WO 2009057622 A1 WO2009057622 A1 WO 2009057622A1
Authority
WO
WIPO (PCT)
Prior art keywords
growth hormone
human growth
nucleotide sequence
substitution
efficiency
Prior art date
Application number
PCT/JP2008/069616
Other languages
French (fr)
Japanese (ja)
Inventor
Hiroyuki Sonoda
Atsushi Sugimura
Original Assignee
Jcr Pharmaceuticals Co., 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 Jcr Pharmaceuticals Co., Ltd. filed Critical Jcr Pharmaceuticals Co., Ltd.
Publication of WO2009057622A1 publication Critical patent/WO2009057622A1/en

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Classifications

    • CCHEMISTRY; METALLURGY
    • C07ORGANIC CHEMISTRY
    • C07KPEPTIDES
    • C07K14/00Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof
    • C07K14/435Peptides having more than 20 amino acids; Gastrins; Somatostatins; Melanotropins; Derivatives thereof from animals; from humans
    • C07K14/575Hormones
    • C07K14/61Growth hormone [GH], i.e. somatotropin
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61PSPECIFIC THERAPEUTIC ACTIVITY OF CHEMICAL COMPOUNDS OR MEDICINAL PREPARATIONS
    • A61P5/00Drugs for disorders of the endocrine system
    • A61P5/06Drugs for disorders of the endocrine system of the anterior pituitary hormones, e.g. TSH, ACTH, FSH, LH, PRL, GH
    • AHUMAN NECESSITIES
    • A61MEDICAL OR VETERINARY SCIENCE; HYGIENE
    • A61KPREPARATIONS FOR MEDICAL, DENTAL OR TOILETRY PURPOSES
    • A61K38/00Medicinal preparations containing peptides

Landscapes

  • Health & Medical Sciences (AREA)
  • Chemical & Material Sciences (AREA)
  • Endocrinology (AREA)
  • Life Sciences & Earth Sciences (AREA)
  • Organic Chemistry (AREA)
  • Medicinal Chemistry (AREA)
  • General Health & Medical Sciences (AREA)
  • Biochemistry (AREA)
  • Chemical Kinetics & Catalysis (AREA)
  • Gastroenterology & Hepatology (AREA)
  • Genetics & Genomics (AREA)
  • Zoology (AREA)
  • Molecular Biology (AREA)
  • Proteomics, Peptides & Aminoacids (AREA)
  • Toxicology (AREA)
  • Engineering & Computer Science (AREA)
  • Bioinformatics & Cheminformatics (AREA)
  • Diabetes (AREA)
  • Biophysics (AREA)
  • General Chemical & Material Sciences (AREA)
  • Nuclear Medicine, Radiotherapy & Molecular Imaging (AREA)
  • Pharmacology & Pharmacy (AREA)
  • Animal Behavior & Ethology (AREA)
  • Public Health (AREA)
  • Veterinary Medicine (AREA)
  • Preparation Of Compounds By Using Micro-Organisms (AREA)
  • Micro-Organisms Or Cultivation Processes Thereof (AREA)
  • Medicines That Contain Protein Lipid Enzymes And Other Medicines (AREA)

Abstract

Disclosed are a means and a method for increasing the efficiency of the expression of human growth hormone in a transformed Escherichia coli cell and also increasing the rate of collection of an active protein from an inclusion body produced. Specifically disclosed are: an human growth hormone expression vector which has, integrated therein, DNA comprising any one nucleotide sequence selected from the group consisting of the nucleotide sequence depicted in SEQ ID NO:3 and a nucleotide sequence having such substitution of a nucleotide in the nucleotide sequence depicted in SEQ ID NO:3 that the GC% in the nucleotide sequence having the substitution falls within the range from 48 to 52% and no modification is caused in an amino acid sequence encoded by the nucleotide sequence having the substitution, and which further has PL promoter and PR promoter and a temperature-sensitive repressor gene; a method for producing human growth hormone by using an Escherichia coli cell which has been transformed with the expression vector; and a method for producing an active form of human growth hormone from human growth hormone produced in the form of an inclusion body.
PCT/JP2008/069616 2007-10-29 2008-10-29 Method for production of human growth hormone improved in efficiency WO2009057622A1 (en)

Applications Claiming Priority (2)

Application Number Priority Date Filing Date Title
JP2007-280912 2007-10-29
JP2007280912A JP4886654B2 (en) 2007-10-29 2007-10-29 Efficient production method of human growth hormone

Publications (1)

Publication Number Publication Date
WO2009057622A1 true WO2009057622A1 (en) 2009-05-07

Family

ID=40591011

Family Applications (1)

Application Number Title Priority Date Filing Date
PCT/JP2008/069616 WO2009057622A1 (en) 2007-10-29 2008-10-29 Method for production of human growth hormone improved in efficiency

Country Status (2)

Country Link
JP (1) JP4886654B2 (en)
WO (1) WO2009057622A1 (en)

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3135686A1 (en) * 2015-08-28 2017-03-01 Latvian Biomedical Research and Study Centre Novel recombinant cyclized human growth hormone

Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH01168298A (en) * 1987-12-23 1989-07-03 Tosoh Corp Activation of insoluble different proteins
JPH02265490A (en) * 1988-11-11 1990-10-30 Boehringer Mannheim Gmbh Expression of recombinant gene, expressive vector and expressive accessory vector
JPH07303492A (en) * 1990-02-28 1995-11-21 Monsanto Co Method of refining somatotropin monomer
JP2004504847A (en) * 2000-07-27 2004-02-19 ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング Production of recombinant proteins in prokaryotic host cells

Patent Citations (4)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
JPH01168298A (en) * 1987-12-23 1989-07-03 Tosoh Corp Activation of insoluble different proteins
JPH02265490A (en) * 1988-11-11 1990-10-30 Boehringer Mannheim Gmbh Expression of recombinant gene, expressive vector and expressive accessory vector
JPH07303492A (en) * 1990-02-28 1995-11-21 Monsanto Co Method of refining somatotropin monomer
JP2004504847A (en) * 2000-07-27 2004-02-19 ベーリンガー インゲルハイム インターナショナル ゲゼルシャフト ミット ベシュレンクテル ハフツング Production of recombinant proteins in prokaryotic host cells

Non-Patent Citations (13)

* Cited by examiner, † Cited by third party
Title
ARMAREGO W.L. ET AL.: "High-level expression of human dihydropteridine reductase (EC 1.6.99.7), without N-terminal amino acid protection, in Escherichia coli", BIOCHEM. J., vol. 261, no. 1, 1989, pages 265 - 268 *
ELVIN C.M. ET AL.: "Modified bacteriophage lambda promoter vectors for overproduction of proteins in Escherichia coli", GENE, vol. 87, no. 1, 1990, pages 123 - 126 *
IKEHARA M ET AL.: "Synthesis of a gene for human growth hormone and its expression in Escherichia coli.", PROC. NATL. ACAD. SCI. USA, vol. 81, no. 19, 1984, pages 5956 - 5960 *
JUNJIE B. ET AL.: "Cloning of cDNA for common carp GH and its expression in prokaryocyte", CHINESE JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 15, no. 3, 1999, pages 409 - 412 *
JUNJIE B. ET AL.: "Cloning of cDNA for porcine GH and its expression in E.coli", JOURNAL OF HUAZHONG AGRICULTURAL UNIVERSITY, vol. 20, no. 2, 2001, pages 99 - 102 *
MAKRIDES S.C.: "Strategies for achieving high- level expression of genes in Escherichia coli", MICROBIOL. REV., vol. 60, no. 3, 1996, pages 512 - 538 *
MUKHIJA R ET AL.: "High-level production and one-step purification of biologically active human growth hormone in Escherichia coli", GENE, vol. 165, no. 2, 1995, pages 303 - 306 *
NAKAMURA Y. ET AL.: "Codon usage tabulated from international DNA sequence databases: status for the year 2000", NUCLEIC ACIDS RES., vol. 28, no. 1, 2000, pages 292 *
ROYTRAKUL S. ET AL.: "A rapid and simple method for construction and expression of a synthetic human growth hormone gene in Escherichia coli.", JOURNAL OF BIOCHEMISTRY AND MOLECULAR BIOLOGY, vol. 34, no. 6, 2001, pages 502 - 508 *
SINGH SM ET AL.: "Solubilization and refolding of bacterial inclusion body proteins", J. BIOSCI. BIOENG., vol. 99, no. 4, 2005, pages 303 - 310 *
SONODA H. ET AL.: "Improved solubilization of recombinant human growth hormone inclusion body produced in Escherichia coli", BIOSCI. BIOTECHNOL. BIOCHEM., vol. 72, no. 10, 23 October 2008 (2008-10-23), pages 2675 - 2680 *
STAMFORD N.P. ET AL.: "Enriched sources of Escherichia coli replication proteins. The dnaG primase is a zinc metalloprotein", BIOCHIM. BIOPHYS. ACTA, vol. 1132, no. 1, 1992, pages 17 - 25 *
TOKUNAGA T. ET AL.: "Expression of a synthetic human growth hormone gene in yeast", GENE, vol. 39, no. 1, 1985, pages 117 - 120 *

Cited By (1)

* Cited by examiner, † Cited by third party
Publication number Priority date Publication date Assignee Title
EP3135686A1 (en) * 2015-08-28 2017-03-01 Latvian Biomedical Research and Study Centre Novel recombinant cyclized human growth hormone

Also Published As

Publication number Publication date
JP2009106180A (en) 2009-05-21
JP4886654B2 (en) 2012-02-29

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