Abstract
A variant of erythrocytic pyruvate kinase, observed in a patient with congenital nonspherocytic hemolytic anemia is characterized by the following properties: a 50-percent decrease in hemolysate enzyme activity; increased affinity for phosphoenolpyruvate; decreased FDP activation; decreased ATP inhibition; very important thermal instability; normal urea denaturation; normal affinity for the second substrate ADP; normal pH of optimal activity. At least all these properties should be studied to identify new variants of red cell pyruvate kinase.

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