An inherited variant of mouse sn-glycerol-3-phosphate dehydrogenase detected by isoelectric focusing: genetical and biochemical analyses.

An electrophoretically detectable mutant of sn-glycerol-3-phosphate dehydrogenase (GPDH) has been found in the offspring of 1-ethyl-1-nitrosourea-treated mice. The banding alteration was detected by isoelectric focusing (IEF) of crude liver extract on polyacrylamide gels. The GPDH alteration is not organ specific. The mutant protein is more positively charged than the wild type. The mutation is codominantly expressed. Heterozygous and homozygous mutants have distinguishable IEF banding patterns. The specific activity of GPDH is not altered by the mutation. The mutated allele causes a greater heat stability to the GPDH protein. Enzymes extracted from the three genotypes are indistinguishable in terms of their pH optima. Gdc-1e is proposed as the allele symbol for the new mutation.