Detail of "6709-57-5"

Reference

Phosphatidic acid biosynthesis in rat liver mitochondria and microsomal fractions

Phosphatidic acid biosynthesis in rat liver mitochondria and microsomal fractions. Regulation of fatty acid positional specificity. Bjerve, Kristian S.; Daae, Ludvig N. W.; Bremer, Jon (Inst. Clin. Biochem., Rikshospitalet, Oslo, Norway). Biochem. 6709-57-5 and 1763-10-6 which are cas registry numbers are also used here. J., 158(2), 249-54 (English) 1976. CODEN: BIJOAK. DOCUMENT TYPE: Journal CA Section: 6 (General Biochemistry) In the formation of phosphatidic acid by rat liver, the preference for palmitic acid at the 1-position was increased by high acyl-CoA concns. in mitochondria, but decreased in microsomes. The preference in mitochondria for linoleic acid at the 2-position of phosphatidic acid was strongly increased by high concns. of lysophosphatidic acid. Acyl-CoA concn. had no effect on the fatty acid specificity at the 2-position. .

In vitro effects of chlorpromazine on glycerol-3-phosphate acyltransferase and 1-acylglycerol-3-phosphate acyltransferase in rat liver microsomes

In vitro effects of chlorpromazine on glycerol-3-phosphate acyltransferase and 1-acylglycerol-3-phosphate acyltransferase in rat liver microsomes. Yada, Ritsuko; Ide, Hayao; Nakazawa, Yasuo (Med. Res. Inst., Tokyo Med.In this study，9067-71-4 is also used. and Dent. Univ., Tokyo 101, Japan). Biochem. Pharmacol., 35(22), 4083-7 (English) 1986. CODEN: BCPCA6. ISSN: 0006-2952. DOCUMENT TYPE: Journal CA Section: 1 (Pharmacology) Section cross-reference(s): 7 The in vitro effects of chlorpromazine [50-53-3] on rat liver glycerol-3-phosphate acyltransferase(EC 2.3.1.15) [9029-96-3] and 1-acylglycerol-3-phosphate acyltransferase(EC 2.3.1.51) [9067-71-4] was studied. Chlorpromazine decreased glycerol-3-phosphate acyltransferase activity in a concn.-dependent manner. The inhibition was competitive with respect to palmitoyl-CoA [1763-10-6] while non-competitive with respect to sn-glycerol-3-phosphate [17989-41-2]. Ki Was detd. to be approx. 0.15 mM with respect to both palmitoyl-CoA and sn-glycerol-3-phosphate. From these results, together with the inhibitory effect of amphiphilic anions and neutral detergents on the enzyme demonstrated by others, it was proposed that the hydrophobic moiety of chlorpromazine competes with acyl-CoA. The activity of 1-acylglycerol-3-phosphate acyltransferase was inhibited by excess of 1-acyl-sn-glycerol-3-phosphate. In the acceptor concn. range where the substrate inhibition was obsd., chlorpromazine showed stimulatory effect on the enzyme activity. At lower concns. of the acceptor, however, chlorpromazine produced marked inhibition of the enzyme activity. From the kinetic anal., the inhibition was found to be uncompetitive with respect to acyl-CoA. It was found that the enzyme was more susceptible to the inhibitory action of chlorpromazine with unsatd. acyl-CoAs than with the satd. species, raising the possibility that chlorpromazine alters the mol. species compn. of phosphatidic acid produced by the acylation reaction. .