牛脾脏CD38/NAD+二硫糖水解酶二聚体的发生。

L Berruet, H Muller-Steffner, F Schuber
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引用次数: 0

摘要

牛脾NAD+糖水解酶是一种与CD38密切相关的外酶,催化NAD+转化为adp -核糖和环adp -核糖,这是一种钙动员代谢产物。我们提出了针对天然酶的多克隆抗体,免疫印迹显示,除了32 kDa的单体外,还存在稳定的二聚体形式。这种二聚化被证明是自发氧化过程的结果,涉及形成一个或几个对还原剂(如2-巯基乙醇)敏感的二硫键。同型二聚体氧化酶,在酶纯化过程的早期步骤中未检测到,具有催化活性。我们的研究结果强调了CD38/NAD+糖水解酶在寡聚和对硫醇的反应性方面的差异,这取决于它们的来源。
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Occurrence of bovine spleen CD38/NAD+glycohydrolase disulfide-linked dimers.

Bovine spleen NAD+glycohydrolase, an ecto-enzyme closely related to CD38, catalyzes the conversion of NAD+ into ADP-ribose and cyclic ADP-ribose, a calcium-mobilizing metabolite. We have raised polyclonal antibodies against the native enzyme which on immunoblots revealed, besides the 32 kDa monomer, the presence of a stable dimeric form. This dimerization was shown to result from a spontaneous oxidative process involving the formation of one or several disulfide bond(s) sensitive to reducing agents such as 2-mercaptoethanol. The homodimeric oxidized enzyme, which was not detected during the early steps of the enzyme purification procedure, was catalytically active. Our results underline the differences, in terms of oligomerization and reactivity towards thiols, between CD38/NAD+glycohydrolases depending on their origin.

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