Purification and characterization of two allelic forms ofl-glycerol 3-phosphate dehydrogenase from inbred strains of mice

✍ Scribed by Leslie P. Kozak

• Publisher: Springer
• Year: 1974
• Tongue: English
• Weight: 496 KB
• Volume: 12
• Category: Article
• ISSN: 0006-2928
• DOI: 10.1007/bf00487529

✦ Synopsis

The half-lives of the enzyme at 50 C were 6 and33 min, respectively, for the BALB/cJ and C57BL/6J strains. Enzyme preparations from the two strains of mice were compared with respect to the following properties and found to be essentially indistinguishable: K m values for dihydroxyacetone phosphate, NADH, L-~-glycerophosphate, and NAD+; maximum velocity; competitive inhibition by inorganic phosphate; pH optimum; energy of activation; eIectrophoretic mobility; molecular weight and subunit molecular weight. From these data, it is concluded that the kinetic properties of the purified enzyme are not the factors responsible for the differences in activity found in crude homogenates of mouse tissues.