Biochemical and immunological studies of three genetic variants of 3-phosphoglycerate kinase 2 from the mouse |
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| Authors: | Chi-Yu Lee Bruna Pegoraro |
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| Affiliation: | (1) Laboratory of Animal Genetics, National Institute of Environmental Health Sciences, 27709 Research Triangle Park, North Carolina;(2) Present address: Department of Electrical Engineering, Duke University, 27706 Durham, North Carolina |
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| 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 that PGK-2B is more heat stable than either PGK-2A or PGK-2C. Enzyme immunoinactivation 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. |
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| Keywords: | genetic variants isozymes PGK biochemical genetics immunology |
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