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人胎盘15-羟基前列腺素脱氢酶的动力学研究。

Kinetic studies on 15-hydroxyprostaglandin dehydrogenase from human placenta.

作者信息

Schlegel W, Greep R O

出版信息

Adv Prostaglandin Thromboxane Res. 1976;1:159-62.

PMID:187034
Abstract

The enzyme system 15-hydroxyprostaglandin dehydrogenase, which catalyzes the oxidation of the 15-hydroxy group of all naturally occurring prostaglandins, has been purified 1,270-fold by isoelectric focusing. Km values have been determined for prostaglandin E2 and NAD+ and were found to be 1 and 44 muM. The overall forward reaction was V1 = 450 nmol/min. Both the product 15-ketoprostaglandin E2 and the metabolite 13,14-dihydro-15-ketoprostaglandin E2 were noncompetitive inhibitors for the enzyme.

摘要

催化所有天然存在的前列腺素15-羟基氧化的酶系统15-羟基前列腺素脱氢酶,已通过等电聚焦纯化了1270倍。已测定前列腺素E2和NAD+的Km值,分别为1μM和44μM。总的正向反应速率V1 = 450 nmol/min。产物15-酮基前列腺素E2和代谢物13,14-二氢-15-酮基前列腺素E2均为该酶的非竞争性抑制剂。

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