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Comparative Enzymologic Study of Catalytic Properties of Brain Cholinesterase of the Mink Mustela vison
Study of preparations of different parts of brain of the American mink Mustela vison Bris. has revealed the highest activity of acetylcholinesterase (AChE) in the caudate nucleus. Using the method of substrate-inhibitor analysis, homogeneity of this AChE preparation has been shown. Acetylthiocholine...
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Published in: | Journal of evolutionary biochemistry and physiology 2003-05, Vol.39 (3), p.306-313 |
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Main Authors: | , , , |
Format: | Article |
Language: | English |
Subjects: | |
Online Access: | Get full text |
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Summary: | Study of preparations of different parts of brain of the American mink Mustela vison Bris. has revealed the highest activity of acetylcholinesterase (AChE) in the caudate nucleus. Using the method of substrate-inhibitor analysis, homogeneity of this AChE preparation has been shown. Acetylthiocholine was hydrolyzed with the highest rate to exceed even acetylcholine, its advantage being also revealed in a^sub c^/K^sub M^ value that reflects to a degree the affinity of the substrate to the enzyme. The study of inhibitory specificity showed no differences of AChE in the human brain and in erythrocytes.[PUBLICATION ABSTRACT] |
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ISSN: | 0022-0930 1608-3202 |
DOI: | 10.1023/A:1026195708804 |