A mutation resulting in increased triosephosphate isomerase activity in Mus musculus.
A mutation resulting in increased triosephosphate isomerase (TPI) activity in blood was recovered in offspring of procarbazine hydrochloride-treated male mice. Breeding experiments indicated a codominant mode of expression. Compared to the wild type, heterozygous and homozygous mutants have mean erythrocyte TPI activities of approximately 140 and 190%, respectively. Besides blood and erythrocytes the increased activity is expressed to a similar degree in spleen, and to a lesser degree in liver, lung, kidney, muscle and brain. Enhanced activity was absent in the heart. Heterozygous and homozygous mutants are viable, fully fertile and exhibit no significant differences in haematological or other physiological traits studied. Biochemical investigations of TPI in both mutant genotypes revealed neither physicochemical nor kinetic differences compared to the wild type. Moreover, immunoinactivation studies showed no difference in the amount of antiplasma required to inactivate a constant amount of TPI activity in all three genotypes, strongly suggesting that the differences in enzyme activity are attributable to differing amounts of enzyme protein expressed per cell. Mapping studies indicated that the mutation is closely linked to the Gapd locus and consequently is located either adjacent to or within the Tpi-1 structural locus. It is hypothesized that the mutation affected a regulatory element contiguous to the Tpi-1 structural locus which acts by increasing the amount of TPI expressed.[1]References
- A mutation resulting in increased triosephosphate isomerase activity in Mus musculus. Merkle, S., Reitmeir, P., Pretsch, W. Genet. Res. (1991) [Pubmed]
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