Abstract
1.1. Biochemical properties of the pyruvate kinase (PK) of an O. limosus crayfish hepatopancreas. abdominal muscle and heart have been investigated.2.2. The PK of the hepatopancreas was characterized by sigmoidal kinetics with phosphoenolpyruvate us substrate and by alla.steric activation under the influence of fructose- 1.6-diphosphate. The PK from the heart and abdominal muscle showed a hyperbolic kinetics with phosphoenolpyruvate, not modified by fructose-1.6-diphosphate.3.3. Adenosinetriphosphate caused the inhibition of the PK activity of the investigated tissues, reversed by the increase in the Mg2+ concentration4.4. The results suggest the existence of two forms of pyruvate kinase in the crayfish tissues
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