EXPLANATION FOR APPARENT LACK OF OUABAIN INHIBITION OF PYRUVATE PRODUCTION IN HEMOLYSATES - BACKWARD PGK REACTION

  • 1 January 1976
    • journal article
    • research article
    • Vol. 47  (3) , 507-512
Abstract
The concept that ouabain-sensitive human membrane (Na+ + K+)-ATPase-generated ADP preferentially serves as the substrate for the phosphoglycerate kinase (PGK) step of erythrocyte glycolysis was reexamined. Membrane ATPase readily provides ADP for and utilizes ATP generated in the pyruvate kinase (PK) step and is ouabain sensitive. Earlier reports in the literature, which suggested that in hemolysates the ATPase reaction facilitating the PK reaction is ouabain-insensitive, are reinterpreted: in crude hemolysates ADP generated in the backward PGK reaction can account for these data. There apparently is no convincing evidence of selective linkage of (Na+ + K+)-ATPase with the PGK reaction.