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Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16.

Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Research Abstract Details 

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  • Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Abstract Text:

    yoshimitsu takakuraYoshimitsu Takakura,hiroshi tsukamotoHiroshi Tsukamoto,takeshi yamamotoTakeshi Yamamoto,yoshimitsu takakuraYoshimitsu Takakura,hiroshi tsukamotoHiroshi Tsukamoto,takeshi yamamotoTakeshi Yamamoto,

    We cloned, expressed and characterized a novel alpha/beta-galactoside alpha2,3-sialyltransferase from Vibrio sp. bacterium JT-FAJ-16. Using a alpha2,3-sialyltransferase gene from a marine bacterium as a probe, a DNA sequence encoding a 402-amino-acid protein was identified from the JT-FAJ-16 genomic library. The protein showed 27.3-64.7% identity to the bacterial sialyltransferases classified into glycosyltransferase family 80. The protein showed sialyltransferase activity when expressed in Escherichia coli. The N-terminal truncated form of the enzyme was amplified in E. coli and its recovered activity was 215.7 unit/l culture medium. It was purified as a single band on SDS-PAGE through the three chromatographic steps. The specific activity of the purified recombinant enzyme reached 57.5 unit/mg protein. The alpha2,3sialylation was confirmed by (1)H- and (13)C-NMR analyses of the reaction products. The enzyme was optimally active at pH 5.5 and at 20 degrees C. Interestingly, the enzyme used both the alpha- and beta-anomers of galactosides as acceptors, suggesting that it can be described as an alpha/beta-galactoside alpha2,3-sialyltransferase. The enzyme had a wide range of acceptor substrate specificities. It transferred N-acetylneuraminic acid (NeuAc) to various monosaccharides and various oligosaccharides, and both N-linked and O-linked asialo-glycoprotein. These results suggest that the enzyme can be used as a powerful tool for the study for glycotechnology.

    Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Publishing Authors By Initials

    y takakuraY Takakura,h tsukamotoH Tsukamoto,t yamamotoT Yamamoto,y takakuraY Takakura,h tsukamotoH Tsukamoto,t yamamotoT Yamamoto,

    For similar abstracts research abstracts see: abstracts research

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    Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 142

    Page Numbers: 403-12

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 2

    MONTH: 08

    YEAR: 2007

    Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Information

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    LANGUAGE: eng

    NlmUniqueID: 376600

    Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16. Keywords Mesh Terms:

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    Grant and Affiliation Information for Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp. JT-FAJ-16.

    AFFILIATION: Glycotechnology Business Unit, Japan Tobacco Inc, 700 Higashibara, Iwata, Shizuoka, Japan. yoshimitsu.takakura@ims.jti.co.jp

    Country: Japan

    Japan Research PublicationJapan Research Publication

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    MEDLINETA: J Biochem (Tokyo)

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    Molecular cloning, expression and properties of an alpha/beta-Galactoside alpha2,3-sialyltransferase from Vibrio sp JT-FAJ-16 Related Publications

     

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