Isozymes of glyceraldehyde‐3‐phosphate dehydrogenase in man and other mammals

Abstract
Multiple electrophoretically distinct forms of glyceraldehyde-3-phosphate dehydrogenase were observed in human and other mammalian [wolf, pig, rabbit, deer mouse, mouse, hamster and rat] tissues. The human isozymes appeared to have essentially the same structural and kinetic properties. An apparent correlation between red-cell age and the relative intensities of the isoenzymes supports the idea that the isozymes arise as a result of post-translational modification of the polypeptide chain. The possibility that a 2nd locus is involved in the determination of these isozymes was discussed.