نتایج جستجو برای: acetyl coa carboxylase

تعداد نتایج: 49768  

Journal: :The Biochemical journal 1977
J C Mackall M D Lane

The process leading to the rise of acetyl-CoA carboxylase activity in rat mammary tissue after the onset of lactation was investigated. The kinetics of change in enzyme activity and enzyme immunotitratable with antibody against avian liver acetyl-CoA carboxylase were determined during the course of lactogenic differentiation. The antibody inactivates and specifically precipitates acetyl-CoA car...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1976
T Kamiryo S Parthasarathy S Numa

The cellular content of acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC 6.4.1.2] in Saccharomyces cerevisiae is reduced by the addition of long-chain fatty acids to the culture medium. Mutant strains of S. cerevisiae defective in acyl-CoA synthetase [acid:CoA ligase (AMP-forming), EC 6.2.1.3] were isolated and used to determine whether fatty acid itself or a metabolit...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1977
P A Watkins D M Tarlow M D Lane

Labeling experiments with chicken liver cell monolayers and suspensions show that glucagon and N6, O2-dibutyryladenosine 3':5'-cyclic monophosphate (dibutyryl cyclic AMP) block fatty acid synthesis from acetate without appreciably affecting cholesterogenesis from acetate or acylglyceride synthesis from palmitate. Neither acetyl-CoA carboxylase [acetyl-CoA:carbon-dioxide ligase (ADP-forming), EC...

Journal: :Biochemical Society transactions 2000
B J Nikolau D J Oliver P S Schnable E S Wurtele

We have characterized the expression of potential acetyl-CoA-generating genes (acetyl-CoA synthetase, pyruvate decarboxylase, acetaldehyde dehydrogenase, plastidic pyruvate dehydrogenase complex and ATP-citrate lyase), and compared these with the expression of acetyl-CoA-metabolizing genes (heteromeric and homomeric acetyl-CoA carboxylase). These comparisons have led to the development of testa...

2014
Chaiyos Sirithanakorn Abdussalam Adina-Zada John C. Wallace Sarawut Jitrapakdee Paul V. Attwood

L-aspartate is a regulatory feedback inhibitor of the biotin-dependent enzyme pyruvate carboxylase in response to increased levels of tricarboxylic acid cycle intermediates. Detailed studies of L-aspartate inhibition of pyruvate carboxylase have been mainly confined to eukaryotic microbial enzymes, and aspects of its mode of action remain unclear. Here we examine its inhibition of the bacterial...

Journal: :The Biochemical journal 1976
D Stansbie R W Brownsey M Crettaz R M Denton

Plasma insulin concentrations in fed rats were altered acutely by administration of glucose or anti-insulin serum. Rates of fatty acid synthesis in adipose tissue and liver were estimated from the incorporation of 3H from 3H2O. In the adipose tissue dehydrogenase and acetyl-CoA carboxylase were evident. In liver, although changes in rates of fatty acid synthesis were found, the initial activity...

Journal: :Journal of Dairy Science 2021

Modulatory effects of l-carnitine, acetate, propionate, and 5-tetradecyloxy-2-furoic acid (TOFA; an inhibitor acetyl-CoA carboxylase) on oxidation esterification [1-14C]-palmitate were studied in hepatocytes isolated from phlorizin-treated control wethers. Our hypotheses that (1) palmitate would be greater sheep injected with phlorizin; (2) l-carnitine increase more (3) acetate propionate decre...

Journal: :The Biochemical journal 1988
K A Walker S M Ridley T Lewis J L Harwood

Fluazifop is a grass-selective herbicide that appears to act by inhibiting fatty acid synthesis de novo in sensitive species. Results from four different types of experiment show that this inhibition is due to an action of fluazifop on acetyl-CoA carboxylase and not on fatty acid synthetase. The acetyl-CoA carboxylase from sensitive barley (Hordeum vulgare), but not from resistant pea (Pisum sa...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1967
E Ryder C Gregolin H C Chang M D Lane

Recent investigations in this laboratory have shownl 2 that the isocitrate(or citrate-) activated form of liver acetyl CoA carboxylase (E.C. 6.4.1.2) is a large protein structure having a molecular weight of about four million. Electron microscopic examination of the carboxylase in the presence of isocitrate reveals' that it has a filamentous structure with dimensions of SG-100 A by up to 5000 ...

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