Results 231 to 240 of about 89,329 (265)

Acetyl coenzyme A concentrations in plant tissues

Journal of Plant Physiology, 2004
Despite the importance of acetyl coenzyme A in many facets of metabolism and the availability of methods for estimation of its concentration, data for acetyl-CoA concentrations in plant tissues have been very scarce. A method using reversed phase HPLC for the quantitative estimation of acetyl-CoA was applied to a variety of plant tissues.
Ajay W, Tumaney, John B, Ohlrogge, Mike, Pollard   +2 more
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Acetyl-coenzyme A hydrolase in blood

International Journal of Biochemistry, 1981
Abstract 1. 1. The existence of acetyl-coenzyme A hydrolase (AcCoA-H) in human blood has been demonstrated for the first time, with highest specific activity in RBCs and lowest in plasma. 2. 2. It has a pH optimum at 8.0. 3. 3. The RBC AcCoA-H inhibited but the plasma AcCoA-H is stimulated by 0.1–0.4 M NaCl.
L L, Hsu, J L, Claghorn
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The origin of chloroplastic acetyl coenzyme A

Archives of Biochemistry and Biophysics, 1981
Abstract Pyruvic dehydrogenase activity has been examined in a number of highly purified leaf organelles. In spinach leaf cell, the major activity is in the mitochrondrion with low activity in isolated chloroplasts. The major source of CO2 derived from pyruvic acid metabolism in the isolated chloroplast is via the acetolactic synthase reaction ...
D J, Murphy, P K, Stumpf
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Acetyl-coenzyme A carboxylase in maize leaves

Archives of Biochemistry and Biophysics, 1981
Abstract Purified chloroplasts from mesophyll and bundle sheath cells of maize leaves have been shown to be the location of acetyl-CoA carboxylase. In disrupted chloroplasts the enzyme was recovered in the stromal fraction, along with protein-bound biotin; acetyl-CoA carboxylase activity did not require a membrane component.
B J, Nikolau, J C, Hawke, C R, Slack
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Fermentative Pyruvate and Acetyl-Coenzyme A Metabolism

EcoSal Plus, 2004
Pyruvate and acetyl-CoA form the backbone of central metabolism. The nonoxidative cleavage of pyruvate to acetyl-CoA and formate by the glycyl radical enzyme pyruvate formate lyase is one of the signature reactions of mixed-acid fermentation in enterobacteria.
R Gary, Sawers, David P, Clark
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REGULATION OF MAMMALIAN ACETYL-COENZYME A CARBOXYLASE

Annual Review of Nutrition, 1997
▪ Abstract  Long-chain fatty acids are involved in all aspects of cellular structure and function. For controlling amounts of fatty acids, cells are endowed with two acetyl-coenzyme A carboxylase (ACC) systems. ACC-α is the rate-limiting enzyme in the biogenesis of long-chain fatty acids, and ACC-β is believed to control mitochondrial fatty acid ...
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Effect of salicylates on acetyl coenzyme a carboxylase

Biochemical Pharmacology, 1979
Abstract The effects of salicylates on rat and chicken liver acetyl-CoA carboxylase were investigated. Acetyl salicylate (2.5 mM) mimicked the activating effect of citrate on rat liver carboxylase if included during the preincubation period. The dissociated inactive form of chicken liver carboxylase could be reconstituted into the partially active ...
U, Dular, K, Dakshinamurti
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Increase in liver acetyl — Coenzyme a during ketosis

Biochemical and Biophysical Research Communications, 1963
Abstract The level of acetyl-CoA in the livers of alloxan diabetic rats rendered ketotic by withdrawal of insulin and administration of adrenal corticoid hormones and of rats made ketotic by fat feeding is 2.5 – 3 times higher than in untreated controls.
O, WIELAND, L, WEISS
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Measurement of acetyl coenzyme A in rat liver

Analytical Biochemistry, 1969
Abstract The estimation of acetyl CoA in rat liver samples by enzymic methods has been investigated with particular reference to the techniques used for obtaining the samples. In the assay it was found necessary to measure the NADH 2 produced in the coupled enzyme reaction fluorometrically and to add internal standards of acetyl CoA to the cuvet at
J, Lumbers, C J, Threlfall, H B, Stoner
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5 Acetyl-Coenzyme A Carboxylase

1987
Publisher Summary This chapter summarizes the regulation of the specific activity of acetyl-CoA carboxylase from animal tissues, especially by phosphorylation. Acetyl-CoA carboxylase derived from both avian and mammalian sources has been shown to be activated under conditions that promote the aggregation of the dimers of the enzyme into linear ...
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