Purification and properties of enolase from carp (Cyprinus carpio). Comparison with enolases from mammals' muscles and yeast.

The enolase (2-phospho-D-glycerate hydrolyase E.C. 4.2.1.11) from carp muscle was obtained, the specific activity--88 U/mg of protein. Km for 2-phosphoglycerate was 0.313 mM and for phosphoenolpyruvate--0.76 mM. The enzyme is active only in the presence of divalent metal ions, Mg2+ being the best activator. The phosphate and fluoride decreased the activity of enzyme. The molecular weight of the dimeric form of enzyme was found to be 93,000. The enzyme is immunologically different from pig muscle enolase.