Genetic variation in erythrocyte NAD levels in the mouse and its effect on glyceraldehyde phosphate dehydrogenase activity and stability.
During a screening of inbred strains for enzyme variation in glycolysis, differences were found in glyceraldehyde phosphate dehydrogenase (GAPDH) activity between C57BL/6J and SM/J mice. Segregation analysis did not reveal unequivocal monogenic inheritance. Dialysis of hemolysates caused decay of enzyme activity, especially in C57BL animals, which could be prevented by the presence of NAD. This led to the finding that erythrocyte NAD levels were threefold higher in SM than C57BL animals and, although additively inherited, did not appear to be monogenic. This is comparable with but independent of the differences and effect of erythrocyte NADP levels on glucose-6 phosphate dehydrogenase activity reported by R. P. Erickson (1974) Biochem. Genet. 11:33] and emphasizes the range of mechanisms that can be involved in the genetic control of enzyme activity in mammalian systems.
D000818:Animals; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000097:blood* / Q000235:genetics; D007526:Isoelectric Point; D051379:Mice; D008815:Mice, Inbred Strains / Q000235:genetics; D009243:NAD / Q000097:blood* / Q000235:genetics; D009249:NADP / Q000097:blood; D013379:Substrate Specificity
D009243:NAD; D009249:NADP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases