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[微粒体NAD-糖水解酶的动力学特性:天然的及用非离子表面活性物质增溶后的]

[Kinetic characteristics of microsomal NAD-glycohydrolase natural and solubilized with a non-ionic surface-active substance].

作者信息

Sestini S, Cinci G, Ricci C

出版信息

Boll Soc Ital Biol Sper. 1982 Apr 30;58(8):450-2.

PMID:6284185
Abstract

Microsomal rat spleen NAD-glycohydrolase was solubilized by Nonidet P40. The solubilized enzyme shows Nicotinamide inhibition and pH dependence at the same extent as unsolubilized microsomal one. It differs from the latter in having a higher affinity for NAD and NADP, and in showing two peaks, instead of one, on electrofocusing: the former with a pH 5 pI without any activity, the latter with a pH 4, 1 pI with a high NAD-ase activity.

摘要

微粒体大鼠脾脏NAD - 糖水解酶通过Nonidet P40溶解。溶解后的酶与未溶解的微粒体酶一样,表现出相同程度的烟酰胺抑制和pH依赖性。它与后者的不同之处在于,对NAD和NADP具有更高的亲和力,并且在等电聚焦时显示出两个峰,而不是一个峰:前者的pH 5等电点无任何活性,后者的pH 4.1等电点具有高NAD酶活性。

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Calf spleen NAD+ glycohydrolase: solubilization, purification, and properties of the intact form of the enzyme.
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