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烟酸酯的酶促水解:血浆与肝脏催化作用的比较

Enzymic hydrolysis of nicotinate esters: comparison between plasma and liver catalysis.

作者信息

Durrer A, Wernly-Chung G N, Boss G, Testa B

机构信息

School of Pharmacy, University of Lausanne, Switzerland.

出版信息

Xenobiotica. 1992 Mar;22(3):273-82. doi: 10.3109/00498259209046639.

DOI:10.3109/00498259209046639
PMID:1496819
Abstract
  1. The enzymic hydrolysis of a wide series of nicotinic acid esters was investigated using human and rat plasma, and purified hog liver carboxylesterase, and compared with previously published data from rat liver microsomes. Esterase activities were always found to obey Michaelis-Menten kinetics. 2. Rat liver microsomal and plasma enzyme velocities were six orders of magnitude smaller than those of purified hog liver carboxylesterase, and three orders smaller than human plasma activities, but the Km values were of the same magnitude. 3. The binding of nicotinate esters to human plasma esterases, and purified hog liver carboxylesterase, appears to depend mainly on hydrophobic and steric factors.
摘要
  1. 使用人和大鼠血浆、纯化的猪肝羧酸酯酶对一系列烟酸酯的酶促水解进行了研究,并与先前发表的大鼠肝微粒体数据进行了比较。酯酶活性始终符合米氏动力学。2. 大鼠肝微粒体和血浆酶的速度比纯化的猪肝羧酸酯酶小六个数量级,比人血浆活性小三个数量级,但Km值处于相同量级。3. 烟酸酯与人血浆酯酶和纯化的猪肝羧酸酯酶的结合似乎主要取决于疏水和空间因素。

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