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 characterization of phosphoglucose isomerase and genetic variants from mouse andDrosophila melanogaster
โ Scribed by Daniel Charles; Chi-Yu Lee
- Publisher
- Springer
- Year
- 1980
- Tongue
- English
- Weight
- 722 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0300-8177
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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. Compa