Abstract
Phosphofructokinase (PFK) has been previously suggested as being responsible for the differences in glycolytic 2,3-diphosphoglycerate (DPG) levels in two inbred populations of Long-Evans hooded rats. The enzyme's in vivo activity appears to be greater in animals with high levels of DPG and lower in those with low levels of this metabolite. In an initial attempt to characterize any structural differences in the red cell PFK enzyme of the two rat strains, we have performed a heat inactivation study. Our results show that the red cell PFK in animals with low levels of DPG is more heat labile relative to that in animals with high levels. This data provides further evidence that the genetic locus determining DPG levels may be the PFK structural gene.
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