Comparison of the properties of two forms of pyruvate kinase in rat liver and determination of their separate activities during development.
1. Two forms of hepatic pyruvate kinase, designated type L and type M, were distinguished on the basis of kinetic, chromatographic, electrophoretic and immunological criteria. They were partially purified and their properties compared with each other and with the purified enzyme from skeletal muscle. 2. In contrast with type L, the type M enzyme showed no marked evidence of co-operative interactions with phosphoenolpyruvate and was not stimulated by fructose diphosphate. 3. The activity profiles of type L and type M enzymes were determined in developing rat liver by utilizing differences in the kinetic properties of the two forms. The high activity of type M enzyme in the early foetal rat decreased in late gestation and immediately after birth to reach a low value, which remained essentially constant for the remainder of the developmental period. The activity of type L enzyme, in contrast, was low in the early foetal and neonatal liver but increased markedly at the onset of weaning. 4. Possible roles of the two forms of hepatic pyruvate kinase in the control of glycolysis and gluconeogenesis are discussed.
D000645:Ammonium Sulfate; D000818:Animals; D000831:Animals, Newborn; D002482:Cellulose; D002848:Chromatography, DEAE-Cellulose; D004586:Electrophoresis; D005333:Fetus / Q000201:enzymology; D005943:Gluconeogenesis; D006019:Glycolysis; D005779:Immunodiffusion; D007700:Kinetics; D008099:Liver / Q000201:enzymology* / Q000254:growth & development; D011770:Pyruvate Kinase / Q000302:isolation & purification*; D051381:Rats
D002482:Cellulose; D011770:Pyruvate Kinase; D000645:Ammonium Sulfate