Explanation for the apparent lack of ouabain inhibition of pyruvate
production in hemolysates: the "backward" PGK reaction
RK Chillar and E Beutler
The concept that ouabain-sensitive membrane (Na+ + K+)-ATPase-generated
adenosine diphosphate (ADP) preferentially serves as the substrate for the
phosphoglycerate kinase (PGK) step of erythrocyte glycolysis has been
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 have 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. We conclude that there is no
convincing evidence of selective linkage of (Na+ + K+)-ATPase with the PGK
reaction.
Volume 47,
Issue 3,
pp. 507-512,
03/01/1976
Copyright © 1976 by The American Society of Hematology
