MEDIUM EFFECTS IN ENZYME SPECIFICITY

被引:3
作者
AAVIKSAAR, A
机构
[1] Estonian Acad of Sciences, Russia
来源
JOURNAL OF MOLECULAR CATALYSIS | 1988年 / 47卷 / 2-3期
关键词
Biochemistry - Chemical Reactions--Reaction Kinetics - Salts--Solutions - Solvents - Substrates--Solubility;
D O I
10.1016/0304-5102(88)85050-8
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
It is shown that chymotrypsin loses its hydrophobic selectivity in lipophilic media and in concentrated salt solutions has a selectivity higher than in water, in accordance with the equation developed for quantitative description of these changes. The results agree with the assumption that the chymotrypsin specificity against nonpolar substrates and inhibitors is determined by their partition between the enzyme active site microphase and the reaction medium, analogously to the partition of these compounds in the octanol-water model system.
引用
收藏
页码:265 / 270
页数:6
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