نتایج جستجو برای: hydroxymethylglutaryl

تعداد نتایج: 2575  

Journal: :The Biochemical journal 1970
G D Baird K G Hibbitt J Lee

1. The activities of acetoacetyl-CoA thiolase, hydroxymethylglutaryl-CoA synthase and lyase and acetoacetyl-CoA deacylase were measured in homogenates of samples of liver, rumen epithelium (long papillae), kidney and lactating mammary gland derived from slaughtered cows. 2. The activities of the four enzymes in bovine liver were similar to the activities previously reported for the correspondin...

Journal: :The Journal of Japan Atherosclerosis Society 1996

2005
Konstantinos A. MITROPOULOS

The activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase (hydroxymethylglutaryl-CoA reductase) was considerably inhibited during incubation with ATP + Mg2+. The inactivated enzyme was reactivated on further incubation with partially purified cytosolic phosphoprotein phosphatase. The inactivation was associated with a decrease in the apparent Km of the reductase for hydroxymethylglutaryl-...

Journal: :The Biochemical journal 1968
D H Williamson M W Bates H A Krebs

1. The activities of hydroxymethylglutaryl-CoA synthase and lyase in rat liver were found to be two- to 15-fold greater than those reported by other authors under similar conditions. 2. When expressed on the basis of body weight, no appreciable differences were found between the activities of hydroxymethylglutaryl-CoA synthase in whole homogenates of livers from normal and starved rats. The syn...

Journal: :The Journal of biological chemistry 1989
D Serra G Asins V E Calvet F G Hegardt

A heat-stable protein inhibitor of the hydroxymethylglutaryl-CoA reductase phosphatase 2A activity has been identified and purified to homogeneity, as judged by polyacrylamide gel electrophoresis. The apparent molecular mass was 20,000 Da. The protein lost its inhibitory properties when incubated with trypsin or treated with ethanol. The inhibitor protein does not inhibit type 1 phosphatase whe...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1996
R Y Hampton A Koning R Wright J Rine

To test the utility of green fluorescent protein (GFP) as an in vivo reporter protein when fused to a membrane domain, we made a fusion protein between yeast hydroxymethylglutaryl-CoA reductase and GFP. Fusion proteins displayed spatial localization and regulated degradation consistent with the native hydroxymethylglutaryl-CoA reductase proteins. Thus, GFP should be useful in the study of both ...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1987
G Gil J R Smith J L Goldstein M S Brown

3-Hydroxy-3-methylglutaryl coenzyme A synthase (hydroxymethylglutaryl-CoA synthase, EC 4.1.3.5) is a negatively regulated enzyme in the synthetic pathway for cholesterol, isopentenyl tRNA, and other isoprenoids. The 5'-untranslated region of the mRNA for Chinese hamster hydroxymethylglutaryl-CoA synthase contains an optional exon of 59 nucleotides located 10 nucleotides upstream of the translat...

Journal: :iranian journal of basic medical sciences 0
mohammad reza haeri department of clinical biochemistry, school of medicine, qom university of medical sciences, qom, iran institute for health research and policy, london metropolitan university, london, united kingdom kenneth white institute for health research and policy, london metropolitan university, london, united kingdom mohammad qharebeglou islamic azad university, qom branch, qom-iran malek moein ansar department of clinical biochemistry, school of medicine, guilan university of medical sciences, rasht, iran

objective(s):isoprenoid biosynthesis is a key metabolic pathway to produce a wide variety of biomolecules such as cholesterol and carotenoids, which target cell membranes. on the other hand, it has been reported that statins known as inhibitors of isoprenoid biosynthesis and cholesterol lowering agents, may have a direct antimicrobial effect on the some bacteria. the exact action of statins in ...

Journal: :The Biochemical journal 1972
S J Henning F J Hird

1. When studied in vitro, tissue from the caecum and the proximal colon of rabbits converted butyrate into ketone bodies. The conversion was similar to that observed with liver slices. The ketogenic activity was associated with the mucosa rather than the muscle of the gut wall and, in the colon, diminished as the distance from the caecal-colonic junction increased. 2. Tissue from the wall of th...

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