| Literature DB >> 94263 |
Abstract
Three electrophoretic variants of 3-phosphoglycerate kinase 2 (PGK-2A,PGK-2B, and PGK-2C) were purified from DBA/2J, C3H/HeJ, and C57L/J mice, respectively. PGK-2C exhibits only 2% of the specific activity of PGK-2A and PGK-2B in the reaction leading to the formation of 1,3-diphosphoglycerate. Compared to PGK-2A and PGK-2B, PGK-2C exhibits broader coenzyme specificity and lower Kms for substrate and coenzymes. Incubation at 45C revealed immunionactivation and double immunodiffusion studies showed that mice carrying any one of these three PGK-2 alleles have similar amounts of proteins for PGK-1 and PGK-2 in testes. The results of these studies suggest that low PGK-2C activity in C57L/J mice is a result of a structural rather than a regulatory gene mutation.Entities:
Mesh:
Substances:
Year: 1979 PMID: 94263 DOI: 10.1007/bf00502123
Source DB: PubMed Journal: Biochem Genet ISSN: 0006-2928 Impact factor: 1.890