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    Please use this identifier to cite or link to this item: http://ir.cnu.edu.tw/handle/310902800/27057

    標題: The Purification and the Catalytic Properties of Purple Acid Phosphatase from Bovine Spleen
    作者: Shieu-Fun, S.Lin
    貢獻者: 藥學科
    日期: 1982
    上傳時間: 2013-10-25 09:22:27 (UTC+8)
    摘要: The existing purification procedure for purple acid phosphatase from bovine spleen was relatively inefficient and has been extended using cellulose phosphate chromatography. The recovery is much higher than that obtained with other tecbniques. The purity is increased by two and a half fold.
    The Michaelis-Menten constant, Km, for p-nitrophenyl phosphate has been found to be 2.0 mM. A plot of 1/Vo versus 1/(S) according to the Lineweaver-Burk equation was used to calculate the Km.
    The relationship between the structural features of inhibitors and the binding specificity of the enzyme is investigated through the inhibition studies of the structural aoalogues of the substrate, PNPP. The results suggest that the binding specificity is not related to the charge distribution on the aromatic moieties of the structual analogues, but related to the nature of phosphorus linkage.
    A catalytic reaction pathway is postulated from the products inhibition studies.
    關聯: 嘉南學報 8, pp.11-22
    Appears in Collections:[嘉南學報] 8 期 (1982)
    [藥學系(所)] 期刊論文

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