منابع مشابه
Regulation of hydroxymethylglutaryl-CoA reductase in rat leukocytes.
Methods were developed for the assay of hydroxymethylglutaryl-CoA reductase (NADPH) activity in microsomes from rat leukocytes. The activity in freshly isolated leukocytes is low compared to rat liver but can be assayed reliably. The patterns of response of leukocyte reductase in the assay to variation in substrate concentration, protein concentration, and time mimic those of rat liver reductas...
متن کاملA hydroxymethylglutaryl-CoA reductase inhibitor synthesized by yeasts.
Screening of different yeast species showed that they are able to synthesize hydroxymethylglutaryl-CoA (HMGCoA) reductase inhibitors. Crude methanol extracts and the purified inhibitors from Pichia labacensis and Candida cariosilignicola were tested for their biological activity on the solubilized microsomal HMGCoA reductase from Chinese hamster ovary cells. Identification of the inhibitors was...
متن کاملAngiotensin converting enzyme (ACE) and HydroxyMethylGlutaryl-CoA (HMG-CoA) reductase inhibitors in the forefront of pharmacology of endothelium.
Healthy endothelium is essential for undisturbed functioning of the cardiovascular system, while endothelial dysfunction leads to its various pathologies. For example endothelial dysfunction precedes clinical symptoms of atherothrombosis, such as acute coronary syndrome, ischemic stroke, peripheral arterial disease or diabetic microangiopathies e.g. retinopathy and nephropathy. Accordingly, pha...
متن کاملTotal hydroxymethylglutaryl CoA reductase activity in the small intestine and liver of insulin-deficient rats.
We examined the effect of streptozotocin-induced diabetes on the rate-limiting enzyme in cholesterol synthesis, 3-hydroxy-3-methylglutaryl CoA reductase (EC 1.1.1.34), in liver and small intestine of rats. During the acute phase of insulin deficiency (first day), food intake, plasma cholesterol, and reductase specific activity in liver all decreased. By 3 days, food intake, plasma cholesterol, ...
متن کاملRegulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system.
Protein phosphatase C was purified 1500-fold from rat liver by a six-step procedure including a fractionation step with 80% ethanol at room temperature and two successive chromatographic separations on DEAESephadex. This preparation restored hydrox~ethyl glutaryl-CoA (HMG-CoA) reductase activity in liver microsomes pretreated with MgATP and also inactivated HMG-CoA reductase kinase. The relativ...
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ژورنال
عنوان ژورنال: The Journal of Japan Atherosclerosis Society
سال: 1996
ISSN: 0386-2682,2185-8284
DOI: 10.5551/jat1973.23.7-8_389