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Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris.

Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Research Abstract Details 

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  • Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Abstract Text:

    jin-ha leeJin-Ha Lee,saori saitoSaori Saito,haruhide moriHaruhide Mori,mamoru nishimotoMamoru Nishimoto,masayuki okuyamaMasayuki Okuyama,doman kimDoman Kim,jintanart wongchawalitJintanart Wongchawalit,atsuo kimuraAtsuo Kimura,seiya chibaSeiya Chiba,jin-ha leeJin-Ha Lee,saori saitoSaori Saito,haruhide moriHaruhide Mori,mamoru nishimotoMamoru Nishimoto,masayuki okuyamaMasayuki Okuyama,doman kimDoman Kim,jintanart wongchawalitJintanart Wongchawalit,atsuo kimuraAtsuo Kimura,seiya chibaSeiya Chiba,

    cDNA encoding the bound type trehalase of the European honeybee was cloned. The cDNA (3,001 bp) contained the long 5' untranslated region (UTR) of 869 bp, and the 3' UTR of 251 bp including a poly(A) tail, and the open reading frame of 1,881 bp consisting of 626 amino acid residues. The Mr of the mature enzyme comprised of 591 amino acids, excluded a signal sequence of 35 amino acid residues, was 69,177. Six peptide sequences analyzed were all found in the deduced amino acid sequence. The amino acid sequence exhibited high identity with trehalases belonging to glycoside hydrolase family 37. A putative transmembrane region similar to trehalase-2 of the silkworm was found in the C-terminal amino acid sequence. Recombinant enzyme of the trehalase was expressed in the methylotrophic yeast Pichia pastoris as host, and displayed properties identical to those of the native enzyme except for higher sugar chain contents. This is the first report of heterologous expression of insect trehalase.

    Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Publishing Authors By Initials

    jh leeJH Lee,s saitoS Saito,h moriH Mori,m nishimotoM Nishimoto,m okuyamaM Okuyama,d kimD Kim,j wongchawalitJ Wongchawalit,a kimuraA Kimura,s chibaS Chiba,jh leeJH Lee,s saitoS Saito,h moriH Mori,m nishimotoM Nishimoto,m okuyamaM Okuyama,d kimD Kim,j wongchawalitJ Wongchawalit,a kimuraA Kimura,s chibaS Chiba,

    For similar abstracts research abstracts see: abstracts research

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    Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Bioscience, biotechnology, and biochemistry

    VOLUME: 71

    Page Numbers: 2256-65

    Journal Abbreviation: Biosci. Biotechnol. Biochem.

    ISSN: 0916-8451

    DAY: 7

    MONTH: 09

    YEAR: 2007

    Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Information

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    LANGUAGE: eng

    NlmUniqueID: 9205717

    Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris. Keywords Mesh Terms:

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    Grant and Affiliation Information for Molecular cloning of cDNA for trehalase from the European honeybee, Apis mellifera L., and its heterologous expression in Pichia pastoris.

    AFFILIATION: Division of Applied Bioscience, Research Faculty of Agriculture, Hokkaido University, Sapporo, 060-8589, Japan.

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: Biosci Biotechnol Biochem

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