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兔乳腺中一种胶束特异性棕榈酰转移酶同工酶的动力学

Kinetics of a micelle specific palmitoyltransferase isoenzyme of rabbit mammary gland.

作者信息

Caffrey M, Kinsella J E

出版信息

Lipids. 1977 Jul;12(7):556-62. doi: 10.1007/BF02533381.

Abstract

Palmityl-CoA: monopalmityl-sn-glycerol 3-phosphate palmitoyltransferase [EC 2.3.1. -] in rabbit mammary gland microsomes is composed of two isoenzymic species. The alpha form (LPAT-alpha) is active with monomeric substrates and inhibited by micelles while the beta form (LPAT-beta) is active only with micelles. By combining the effects of time, temperature, and Tween 80 which selectively inhibited LPAT-alpha, the substrate saturation curve for the LPAT-beta isoenzyme has been successfully determined. Both theoretical and experimental curves are in good agreement.

摘要

兔乳腺微粒体中的棕榈酰辅酶A:单棕榈酰-sn-甘油3-磷酸棕榈酰转移酶[EC 2.3.1. -]由两种同工酶组成。α型(LPAT-α)对单体底物有活性,并被胶束抑制,而β型(LPAT-β)仅对胶束有活性。通过结合时间、温度和选择性抑制LPAT-α的吐温80的作用,成功测定了LPAT-β同工酶的底物饱和曲线。理论曲线和实验曲线吻合良好。

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