Two electrophoretic variants of phosphoglucose isomerase ( PGI) were purified from whole body extracts of DBA/2J and C5 7BL/6Jmice by a substrate-affinity elution from an 8-(6-aminohexyl) amino-A TP-Sepharose column followed by preparative isoelectric focusing. Both PGI variants were shown to be dim
Biochemical and immunological studies of three genetic variants of 3-phosphoglycerate kinase 2 from the mouse
β Scribed by Chi-Yu Lee; Bruna Pegoraro
- Publisher
- Springer
- Year
- 1979
- Tongue
- English
- Weight
- 666 KB
- Volume
- 17
- Category
- Article
- ISSN
- 0006-2928
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β¦ Synopsis
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.
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