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人精浆中单胺氧化酶的生化特性及动力学参数

Biochemical properties and kinetic parameters of monoamine oxydase in human seminal plasma.

作者信息

Roberge A G, Moufarege A, Lavoie J, Roberge C, Tremblay R R

出版信息

Int J Fertil. 1984;29(3):180-5.

PMID:6152258
Abstract

The present study demonstrates that monoamine oxydase (MAO) is present in the human seminal plasma and that its activity was higher in infertile than in fertile men. The Km and Vmax of the enzyme were, respectively, 3.0 X 10(-3) M and 625 eta mol of deaminated 5-HT mg of prot-1 min-1. The enzyme was activated by pyridoxal-5' phosphate but inhibited by usual MAO inhibitors such as pargyline-HCl, iproniazid-PO4 and clorgyline. These findings suggest a relationship between the synthesis and degradation of biogenic amines and testicular function.

摘要

本研究表明,单胺氧化酶(MAO)存在于人类精浆中,且其活性在不育男性中高于生育男性。该酶的米氏常数(Km)和最大反应速度(Vmax)分别为3.0×10⁻³M和625纳摩尔脱氨基5-羟色胺/毫克蛋白⁻¹分钟⁻¹。该酶被磷酸吡哆醛激活,但被常规的单胺氧化酶抑制剂如盐酸帕吉林、异烟肼-磷酸和氯吉兰抑制。这些发现提示生物胺的合成与降解和睾丸功能之间存在关联。

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