[The activity of beta-hydroxy-beta-methylglutaryl-CoA reductase in the soluble fraction of rat liver].
Assay conditions are worked out for determination of activity of beta-hydroxy-beta-methylglutaryl-CoA reductase (HMG-CoA reductase) in 140.000 g supernatant fraction of the rat liver. Some kinetic properties of the enzyme are studied: the activity dependency on the incubation time, protein concentration, pH, glutathione, dithiothreitol and HMG-CoA contents in the incubation medium. The effect of Triton WR 1339 on the activity of HMG-CoA reductase in the liver 140.000 g supernatant and microsomal fractions is comparatively studied. Diurnal activity variations of soluble and microsomal enzymes are also investigated. It is suggested that the rat liver HMG-CoA reductase in the 140.000 g supernatant fraction is not identical to the enzyme located in the microsomal fraction.
[The activity of beta-hydroxy-beta-methylglutaryl-CoA reductase in the soluble fraction of rat liver]. Assay conditions are worked out for determination of activity of beta-hydroxy-beta-methylglutaryl-CoA reductase (HMG-CoA reductase) in 140.000 g supernatant fraction of the rat liver. Some kinetic properties of the enzyme are studied: the activity dependency on the incubation time, protein concentration, pH, glutathione, dithiothreitol and HMG-CoA contents in the incubation medium. The effect of Triton WR 1339 on the activity of HMG-CoA reductase in the liver 140.000 g supernatant and microsomal fractions is comparatively studied. Diurnal activity variations of soluble and microsomal enzymes are also investigated. It is suggested that the rat liver HMG-CoA reductase in the 140.000 g supernatant fraction is not identical to the enzyme located in the microsomal fraction.