Comparative Enzymologic Study of Catalytic Properties of Blood Serum Cholinesterase of the American Mink Mustela vison

Comparative enzymologic study of catalytic properties of cholinesterase (ChE) in blood serum of the American mink Mustela vison Schr. has revealed several peculiarities of this enzyme. First, using the method of substrate-inhibitor analysis, homogeneity of the ChE preparation has been established, i...

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Bibliographic Details
Published in:Journal of evolutionary biochemistry and physiology 2002-07, Vol.38 (4), p.401
Main Authors: Rozengart, E V, Khovanskikh, A E, Basova, N E, Moralev, S N
Format: Article
Language:English
Subjects:
Animal behavior
Fresh water
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Summary:Comparative enzymologic study of catalytic properties of cholinesterase (ChE) in blood serum of the American mink Mustela vison Schr. has revealed several peculiarities of this enzyme. First, using the method of substrate-inhibitor analysis, homogeneity of the ChE preparation has been established, i.e. only one ChE has been found in mink serum. Second, the rate of acetylcholine hydrolysis was higher than of thiocholine substrates, among which propionylthiocholine was hydrolyzed at the highest rate. Third, propionylthiocholine had the highest V/K^sub M^ value that reflects to a degree affinity of the substrate to enzyme. Fourth, the phenomenon of "substrate inhibition," which is not inherent for mammalian serum cholinesterases, is revealed and kinetically analyzed. Fifth, study of inhibitory specificity has not revealed differences of the mink serum ChE from other serum ChE.[PUBLICATION ABSTRACT]
ISSN:0022-0930
1608-3202
DOI:10.1023/A:1021145602100