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Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160.

Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Research Abstract Details 

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  • Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Abstract Text:

    t yamamotoT Yamamoto,m nakashizukaM Nakashizuka,h kodamaH Kodama,y kajiharaY Kajihara,i teradaI Terada,

    A bacterial sialyltransferase, named sialyltransferase 0160, was purified from a marine bacterium that had been isolated from seawater from Sagami Bay, Kanagawa. This strain has been identified as Photobacterium damsela, and named P. damsela JT0160. Sialyltransferase 0160 was purified 688-fold to homogeneity from the crude extract of the cells with a yield of 19% using a combination of anion exchange chromatography, hydroxyapatite chromatography, gel filtration chromatography, and affinity chromatography. The purified enzyme migrated as a single band (61 kDa) on sodium dodecyl sulfate-polyacrylamide gel. This sialyltransferase was found to be a beta-galactoside alpha 2,6-sialyltransferase [EC 2.4.99.1] which catalyzes the incorporation of NeuAc from CMP-NeuAc into the galactose residue of the carbohydrate chain at position 6 on the basis of an analysis of the enzymatic reaction products with HPLC, 1H-, 13C-NMR spectroscopy, and fast atom bombardment mass spectroscopy.

    Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Publishing Authors By Initials

    t yamamotoT Yamamoto,m nakashizukaM Nakashizuka,h kodamaH Kodama,y kajiharaY Kajihara,i teradaI Terada,

    For similar environment and public health: environment: environment, controlled: temperature research abstracts see: environment and public health: environment: environment, controlled: temperature research

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    Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Journal of biochemistry

    VOLUME: 120

    Page Numbers: 104-10

    Journal Abbreviation: J. Biochem.

    ISSN: 0021-924X

    DAY: 19

    MONTH: Jul

    YEAR: 1996

    Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 376600

    Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Keywords Mesh Terms:

    KEYWORDS: Temperature

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160. Information

    Substance Name: beta-D-galactoside alpha 2-6-sialyltrans

    Registry Number: EC 2.4.99.1

    Grant and Affiliation Information for Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160.

    AFFILIATION: Sea Water Science Research Laboratory, Japan Tobacco Inc., Kanagawa.

    Country: JAPAN

    JAPAN Research PublicationJAPAN Research Publication

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    MEDLINETA: J Biochem

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    Purification and characterization of a marine bacterial beta-galactoside alpha 2,6-sialyltransferase from Photobacterium damsela JT0160 Related Publications

     

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