Isozymes of glyceraldehyde-3-phosphate dehydrogenase in man and other mammals.
Multiple electrophoretically distinct forms of glyceraldehyde-3-phosphate dehydrogenase have been observed in human and other mammalian tissues. The human isozymes appear to have essentially the same structural and kinetic properties. An apparent correlation between red-cell age and the relative intensities of the isozymes supports the idea that the isozymes arise as a result of post-translational modification of the polypeptide chain. The possibility that a second locus is involved in the determination of these isozymes is discussed.
D000328:Adult; D000818:Animals; D001665:Binding Sites; D002335:Carnivora; D002462:Cell Membrane / Q000201:enzymology; D006224:Cricetinae; D004912:Erythrocytes / Q000201:enzymology; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000302:isolation & purification*; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification*; D051379:Mice; D008970:Molecular Weight; D009132:Muscles / Q000201:enzymology; D009243:NAD; D011817:Rabbits; D051381:Rats; D013552:Swine
D007527:Isoenzymes; D009243:NAD; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases