Various functional characteristics of enolase isoenzymes in mammals

Considerable stability of beta beta- (muscular) and gamma gamma- (neurospecific) forms to the denaturing influence of neutral salts of alkali metals is shown on purified isoenzymes (alpha alpha-, beta beta-, gamma gamma-forms) of beef brain and rabbit muscle. The rate of influence of these salts on...

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Bibliographic Details
Published in:	Ukrainskij biohimičeskij žurnal Vol. 58; no. 4; p. 72
Main Authors:	Nazarian, K B, Kazarian, B A, Karapetian, N G
Format:	Journal Article
Language:	Russian
Published:	Ukraine 01-07-1986
Subjects:	Animals Brain - enzymology Cattle In Vitro Techniques Isoenzymes - analysis Kinetics Metals - pharmacology Muscles - enzymology Neuroglia - analysis Neurons - enzymology Phosphopyruvate Hydratase - analysis Rabbits
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Summary:	Considerable stability of beta beta- (muscular) and gamma gamma- (neurospecific) forms to the denaturing influence of neutral salts of alkali metals is shown on purified isoenzymes (alpha alpha-, beta beta-, gamma gamma-forms) of beef brain and rabbit muscle. The rate of influence of these salts on the enzymic activity of the mentioned isoenzymes corresponds to the "lyotropic" series. Km of alpha alpha- and gamma gamma-isoenzymes are determined for 2-phosphoglycerate and phosphoenolpyruvate. It is found that alpha alpha-isoenzyme has larger affinity to phosphoenolpyruvate than gamma gamma-isoenzyme and it appears to play an essential role in participation of the given isoenzymes in the glycolysis and glyconeogenesis processes.
ISSN:	0201-8470