BUTYRYLCHOLINESTERASE ACTIVITY TOWARDS LONG-CHAIN ALKANOYLCHOLINES - KINETICS AND MECHANISM

被引：12

作者：

CHELMINSKABERTILSSON, M ^{[1
]}

ALLENMARK, S ^{[1
]}

EDEBO, L ^{[1
]}

机构：

[1] GOTHENBURG UNIV,DEPT ORGAN CHEM,S-41124 GOTHENBURG,SWEDEN

来源：

BIOCHIMICA ET BIOPHYSICA ACTA | 1993年 / 1202卷 / 01期

关键词：

ALKANOYLCHOLINE; BUTYRYLCHOLINESTERASE; HYDROLYSIS; ENZYME KINETICS; ENZYME INHIBITION;

D O I：

10.1016/0167-4838(93)90062-V

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The hydrolysis of long-chain alkanoylcholines catalyzed by butyrylcholinesterase (EC 3.1.1.8) has been studied. Radiolabelled substrates have been used and a radiochromatographic detection method developed earlier has been applied. The long-chain choline esters were found to be excellent substrates for butyrylcholinesterase at low concentrations, with K(m) values lower than those of short-chain analogues. At higher substrate concentrations, however, the hydrolysis reaction is inhibited, due to the formation of mixed micelles between the amphiphilic substrate and the corresponding alkanoic acid formed in the hydrolysis reaction. The inhibition may also partially be the result of conformational changes of the protein following adsorption of the cationic amphiphile. Critical micelle concentrations (CMC) for the long-chain substrates, as well as for mixed micelles, have been determined.

引用

页码：56 / 60

页数：5

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