Erythrocyte isozymes of phosphofructokinase in genetically high- and low-2,3-diphosphoglycerate rats.

A major locus (Dpg) with two alleles (d and D) controls erythrocyte 2,3-diphosphoglycerate (DPG) levels in Long-Evans rats and is closely linked to a locus (Hbb) determining a hemoglobin electrophoretic polymorphism. Glycolytic intermediate levels and phosphofructokinase (PFK) kinetic studies suggest that in vivo PFK activity differences underlie the differences in DPG levels. We report here chromatographic and immunologic evidence that rat erythrocyte PFK is composed of two isozymes which elute from DEAE-Sephadex at positions identical to those of the isozymes in platelets and liver, respectively. The percentage of platelet-type PFK is significantly (P less than 0.05) smaller in low-DPG (dd) hemolysates than in DD hemolysates regardless of hemoglobin phenotype. When hemolysates were prepared in a stabilizing buffer, PFK specific activity was significantly (P less than 0.005) higher in DD rats. These data suggest that the PFK kinetic differences may result from alterations in the isozyme composition of active PFK.