Concomitance of an active and an inactive mutant of red cell pyruvate kinase (PK).
A new mutant red cell PK associated with mild chronic haemolytic anaemia is described. The propositus, double heterozygous for a maternal gene coding for a structural abnormal enzyme and a paternal gene coding for a catalitically inactive enzyme, was suitable for an accurate functional characterization of the PK variant since his erythrocytes contained only one active mutant form of this enzyme. The active isoenzyme was characterized by low activity, decreased affinity for phosphoenolpyruvate, incomplete fructose-1,6-diphosphate activation, increased 'zero-time transition temperature', increased stability to guanidine-HCl and storage at +4 degrees C, increased guanosine-5'-diphosphate and cytidine-5'-diphosphate utilization, altered electrophoretic pattern with a single slow-moving component and abnormal isoelectric point. Affinity for ADP, ATP inhibition, optimum pH, molecular weight of the subunits, antigen concentration and immunological properties were in the normal range.
D000328:Adult; D000745:Anemia, Hemolytic, Congenital / Q000201:enzymology*; D002908:Chronic Disease; D004586:Electrophoresis; D004910:Erythrocyte Membrane / Q000032:analysis; D004912:Erythrocytes / Q000201:enzymology* / Q000378:metabolism; D006579:Heterozygote; D006801:Humans; D007525:Isoelectric Focusing; D007527:Isoenzymes / Q000097:blood; D008297:Male; D009154:Mutation; D011770:Pyruvate Kinase / Q000097:blood / Q000235:genetics*
D007527:Isoenzymes; D011770:Pyruvate Kinase