[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 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.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D002417:Cattle; D066298:In Vitro Techniques; D007527:Isoenzymes / Q000032:analysis*; D007700:Kinetics; D008670:Metals / Q000494:pharmacology; D009132:Muscles / Q000201:enzymology; D009457:Neuroglia / Q000032:analysis; D009474:Neurons / Q000201:enzymology; D010751:Phosphopyruvate Hydratase / Q000032:analysis*; D011817:Rabbits
D007527:Isoenzymes; D008670:Metals; D010751:Phosphopyruvate Hydratase
Nekotorye funktsional'nye kharakteristiki izofermentov enolazy mlekopitaiushchikh.