Detail of "87272-20-6"

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Inhibition of lipid synthesis by bb'-tetramethyl-substituted, C14-C22, a,w-dicarboxylic acids in the rat in vivo

Inhibition of lipid synthesis by bb'-tetramethyl-substituted, C14-C22, a,w-dicarboxylic acids in the rat in vivo. Bar-Tana, Jacob; Rose-Kahn, Gene; Srebnik, Morris (Hadassah Med. Sch., Hebrew Univ., Jerusalem 91010, Israel). 87272-20-6 which is the cas registry number of one of substances is just one of reagents here. J. Biol. Chem., 260(14), 8404-10 (English) 1985. CODEN: JBCHA3. ISSN: 0021-9258. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) bb'-Methyl-substituted a,w-dicarboxylic acids (MEDICA) of C14-C18 chain length inhibited liver lipid synthesis in the rat in vivo. Max. inhibition was obsd. with MEDICA 16 [87272-20-6] amounting to a 50% decrease in fatty acid and cholesterol biosynthesis in the presence of 0.07 and 0.0156% (wt./wt.) of the drug in the diet, resp. Inhibition of lipid biosynthesis by MEDICA 16 involved a redn. in cytosolic acetyl-CoA [72-89-9] content, whereas the C flux from glucose to glycogen, protein, and CO2 remained unaffected. Inhibition of lipogenesis by MEDICA 16 resulted in a 50% decrease in liver and carcass (but not brain) neutral lipid ester content at 0.25% (wt./wt.) of the drug in the diet, as well as in a dose-dependent hypotriglyceridemic effect, with an up to 3-fold redn. in serum triacylglycerols. Inhibition of cholesterogenesis by MEDICA 16 resulted in a hypocholesterolemic effect, with 60 and 45% redns. in (very low d. plus low d. lipoprotein) cholesterol and high d. lipoprotein cholesterol, resp. .

Redox control of catalysis in ATP-citrate lyase from rat liver

Redox control of catalysis in ATP-citrate lyase from rat liver. Wells, Timothy N. C.; Saxty, Barbara A. (Mol. Enzymol. Lab., Smith Kline Beecham, Welwyn, UK). Eur. J. Biochem., 204(1), 249-55 (English) 1992. CODEN: EJBCAI. ISSN: 0014-2956. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) In thiol redox buffers at pH 8.0, rat liver ATP-citrate lyase is in equil. between an oxidized inactive form and a reduced active form. The reduced enzyme is inactivated by oxidized glutathione (GSSG) at a rate of 45 min-1×M-1 and the oxidized enzyme is activated by reduced glutathione (GSH) at a rate of 3.2 min-1×M-1. At redox equil., the enzyme activity depends on the ratio [GSH]2/[GSSG]. The inactivation involves formation of a protein-protein disulfide rather than a protein-glutathione complex. This reaction has Keq = 78 mM for the oxidative reaction. Activity can therefore be controlled by the redox state of the cell, being more active in the fed state than in the oxidatively stressed state. This redox process is also important in the in vitro enzyme assay, where ATP-citrate lyase is in redox equil. with oxygen and either dithiothreitol or 2-mercaptoethanol. Redn. is a two-step process, requiring high concns. of reductant for full activation (30 mM dithiothreitol or 200 mM 2-mercaptoethanol). The enzyme inhibitor, Medica-16 raises the redox equil. const. to greater than 400 mM. It binds more tightly to the oxidized form of the enzyme, with Ki < 40 mM compared to 180 mM for the reduced form.Except for chemicals metioned above, 87272-20-6 and 27025-41-8 are also used. .