نتایج جستجو برای: acetyl coa carboxylase alpha gene

تعداد نتایج: 1331847  

Journal: :Biochemical Society transactions 1994
J W Gronwald

23 Holloway, P. J., Wong, W. W. C., Partridge, H. J., Seaman, D. and Perry, R. B. (1992) Pestic. Sci. 34, 109-118 24 Silcox, D. and Holloway, P. J. (1989) in Adjuvants and Agrochemicals (Chow, P. N. P., Grant, C. A,, Hinshalwood, A. M. and Simundsson, E., eds.), pp. 115-128, CRC Press Inc., Boca Raton, FL 25 Coret, J., Garnbonnet, B., Brabet, F. and Charnel, A. R. (1993) Pestic. Sci. 38, 201-20...

Journal: :Journal of Biological Chemistry 1983

Journal: :Cancer research 2005
Koen Brusselmans Ellen De Schrijver Guido Verhoeven Johannes V Swinnen

Overexpression of lipogenic enzymes is a common characteristic of many cancers. Thus far, studies aimed at the exploration of lipogenic enzymes as targets for cancer intervention have focused on fatty acid synthase (FAS), the enzyme catalyzing the terminal steps in fatty acid synthesis. Chemical inhibition or RNA interference (RNAi)-mediated knockdown of FAS consistently inhibits the growth and...

Journal: :Plant physiology 1984
B J Nikolau E S Wurtele P K Stumpf

Acetyl-CoA carboxylase [acetyl-CoA-carbon dioxide ligase (ADP forming), EC 6.4.1.2] is a biotin-containing enzyme catalyzing the formation of malonyl-CoA. The tissue distribution of this enzyme was determined for leaves of C(3)- and C(4)-plants. The mesophyll tissues of the C(3)-plants Pisum sativum and Allium porrum contained 90% of the leaf acetyl-CoA carboxylase activity, with the epidermal ...

Journal: :The Journal of biological chemistry 1996
U Krause M H Rider L Hue

Incubation of isolated hepatocytes with glutamine or proline or in hypotonic media is known to activate glycogen synthase and acetyl-CoA carboxylase as a result of cell swelling. We report here that the same experimental conditions caused an activation of phosphatidylinositol 3-kinase and p70 ribosomal protein S6 kinase (p70 S6 kinase) but did not modify the activity of p42 mitogen-activated pr...

Journal: :The Journal of biological chemistry 1974
M C Scrutton

Oxalacetate synthesis catalyzed by pyruvate carboxylase from rat liver in the absence of acetyl-CoA exhibits a pH dependence and specificity for activation by univalent and divalent cations similar to that reported previously for acetylCoA-dependent oxalacetate synthesis by this enzyme (McCLURE, W. R., LARDY, H. A., AND KNEIFEL, H. P. (1971) J. Biol. Chem. 246, 3569-3578). Fractionation studies...

2003
MICHAEL C. SCRUTTON

Oxalacetate synthesis catalyzed by pyruvate carboxylase from rat liver in the absence of acetyl-CoA exhibits a pH dependence and specificity for activation by univalent and divalent cations similar to that reported previously for acetylCoA-dependent oxalacetate synthesis by this enzyme (McCLURE, W. R., LARDY, H. A., AND KNEIFEL, H. P. (1971) J. Biol. Chem. 246, 3569-3578). Fractionation studies...

Journal: :Journal of nutritional science and vitaminology 1979
T Tomita R Hasegawa E Hayashi

Neutral lipids, especially triacylglycerols, accumulated due to myo-inositol deficiency both in the cells of Saccharomyces carlsbergensis (Hayashi et al. (1976) J. Biol. Chem., 251, 5759--5769) and in the liver of the rat (Hayashi et al. (1974) Biochim. Biophys. Acta, 360, 134--155). The accumulation of triacylglycerols in the deficient yeast resulted, at least partly, from an enhancement of ac...

Journal: :The Biochemical journal 1987
M G Buckley E A Rath

1. The effect of nutritional status on fatty acid synthesis in brown adipose tissue was compared with the effect of cold-exposure. Fatty acid synthesis was measured in vivo by 3H2O incorporation into tissue lipids. The activities of acetyl-CoA carboxylase and fatty acid synthetase and the tissue concentrations of malonyl-CoA and citrate were assayed. 2. In brown adipose tissue of control mice, ...

Journal: :The Journal of biological chemistry 1972
A G Goodridge

Pahnitoyl-CoA (100 PM), in the presence of albumin (24 mg per ml), inhibited the incorporation of [14C]citrate into fatty acids in a cytosol fraction of chick liver and inhibited the activity of acetyl-CoA carboxylase purified from chick liver. Under similar incubation conditions, pahnitoyl-CoA (ZOO PM) did not inhibit fatty acid synthetase, ATP-citrate lyase, malic enzyme, NADP-linked isocitra...

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