Partial purification and characterization of membrane-associated diacylglycerol kinase of Drosophila heads

Hiroko Inoue*, Tohru Yoshioka, Yoshiki Hotta

*この研究の対応する著者

    研究成果査読

    5 被引用数 (Scopus)

    抄録

    A membrane-associated diacylglycerol kinase of Drosophila heads was purified to near homogeneity from the KCl extract of Drosophila heads. The purification procedure involved chromatography on Q-Sepharose, ammonium sulfate fractionation, Superose 12, hydroxyapatite and ATP-agarose. Sodium dodecyl sulfate-polyacrylamode gel electrophoresis of fractions after the ATP-agarose column chromatography showed that only a 115 kDa protein correlated well with the enzyme activity. The apparent Km values of partially purified DG kinase were 220 μM for ATP and 540 μM for diolein, respectively. The activity of the DG kinase was inhibited by deoxycholate and was not activated by Ca2+.

    本文言語English
    ページ(範囲)219-224
    ページ数6
    ジャーナルBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
    1122
    2
    DOI
    出版ステータスPublished - 1992 7 31

    ASJC Scopus subject areas

    • 生化学
    • 生物理学
    • 分子生物学
    • 構造生物学

    フィンガープリント

    「Partial purification and characterization of membrane-associated diacylglycerol kinase of Drosophila heads」の研究トピックを掘り下げます。これらがまとまってユニークなフィンガープリントを構成します。

    引用スタイル