来自酿酒酵母的膜相关磷脂酰肌醇激酶。
Membrane-associated phosphatidylinositol kinase from Saccharomyces cerevisiae.
作者信息
McKenzie M A, Carman G M
出版信息
J Bacteriol. 1983 Oct;156(1):421-3. doi: 10.1128/jb.156.1.421-423.1983.
Abstract
Membrane-associated phosphatidylinositol kinase (ATP:phosphatidylinositol 4-phosphotransferase, EC 2.7.1.67) was partially purified 93-fold from Saccharomyces cerevisiae. Activity was dependent on magnesium ions (10 mM) and the optimum pH was 8.5. The apparent Km values for ATP and phosphatidylinositol were 0.21 mM and 71 microM, respectively. Activity was stimulated by sodium cholate and inhibited by sodium, potassium, lithium, and fluoride ions.
摘要
膜相关磷脂酰肌醇激酶（ATP：磷脂酰肌醇4-磷酸转移酶，EC 2.7.1.67）从酿酒酵母中部分纯化了93倍。活性依赖于镁离子（10 mM），最适pH为8.5。ATP和磷脂酰肌醇的表观Km值分别为0.21 mM和71 microM。活性受到胆酸钠的刺激，并受到钠、钾、锂和氟离子的抑制。
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