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人胎盘乙醇脱氢酶

Human placental alcohol dehydrogenase.

作者信息

Krasner J, Tischler F, Yaffe S J

出版信息

J Med. 1976;7(3-4):323-32.

PMID:13137
Abstract

Alcohol dehydrogenase derived from the term human placenta was investigated in the 104,000xg supernatant fraction. Kinetic experiments yielded an average Vmax of 6.1 units, a Km of 5X10(-3)M and optimum activity at pH 10.0. Electrophoresis at pH 9.6 in glycine buffer showed four bands, however only two bands were observed at pH 8.6. Properties of this placental enzyme may be unique and its participation in the overall metabolic function of this tissue is unclear.

摘要

对来源于足月人胎盘的乙醇脱氢酶在104,000xg的上清液组分中进行了研究。动力学实验得出平均Vmax为6.1单位,Km为5×10⁻³M,最适活性pH为10.0。在pH 9.6的甘氨酸缓冲液中进行电泳显示有四条带,然而在pH 8.6时仅观察到两条带。这种胎盘酶的特性可能是独特的,其在该组织整体代谢功能中的作用尚不清楚。

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