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1
Increased sensitivity of carnitine palmitoyltransferase I activity to malonyl-CoA inhibition after preincubation of intact rat liver mitochondria with micromolar concentrations of malonyl-CoA in vitro.
Biochem J. 1983 Mar 15;210(3):953-6. doi: 10.1042/bj2100953.
2
Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA.
Biochem J. 1984 Mar 1;218(2):379-86. doi: 10.1042/bj2180379.
3
Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA.
Biochem J. 1984 Dec 15;224(3):1015-8. doi: 10.1042/bj2241015.
4
Reversible sensitization and desensitization of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in isolated rat liver mitochondria. Significance for the mechanism of malonyl-CoA-induced sensitization.
Biochem J. 1983 Sep 15;214(3):1027-30. doi: 10.1042/bj2141027.
5
Effect of pH on malonyl-CoA inhibition of carnitine palmitoyltransferase I.
Biochem J. 1983 May 15;212(2):521-4. doi: 10.1042/bj2120521.
6
Re-evaluation of the interaction of malonyl-CoA with the rat liver mitochondrial carnitine palmitoyltransferase system by using purified outer membranes.
Biochem J. 1990 Apr 1;267(1):85-90. doi: 10.1042/bj2670085.
7
Ethanol increases the sensitivity of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in short-term hepatocyte incubations.
Biochim Biophys Acta. 1989 Apr 26;1002(3):405-8. doi: 10.1016/0005-2760(89)90358-5.
8
Altered sensitivity of carnitine palmitoyltransferase to inhibition by malonyl-CoA in ketotic diabetic rats.
Biochem J. 1984 Apr 1;219(1):337-9. doi: 10.1042/bj2190337.
9
Hysteretic behaviour of carnitine palmitoyltransferase. The effect of preincubation with malonyl-CoA.
Biochem J. 1986 Jun 15;236(3):917-9. doi: 10.1042/bj2360917.
10
Response to starvation of hepatic carnitine palmitoyltransferase activity and its regulation by malonyl-CoA. Sex differences and effects of pregnancy.
Biochem J. 1982 Dec 15;208(3):673-8. doi: 10.1042/bj2080673.
引用本文的文献
1
Evidence against direct involvement of phosphorylation in the activation of carnitine palmitoyltransferase by okadaic acid in rat hepatocytes.
Biochem J. 1994 Jun 15;300 ( Pt 3)(Pt 3):693-9. doi: 10.1042/bj3000693.
2
Time-dependence of inhibition of carnitine palmitoyltransferase I by malonyl-CoA in mitochondria isolated from livers of fed or starved rats. Evidence for transition of the enzyme between states of low and high affinity for malonyl-CoA.
Biochem J. 1984 Mar 1;218(2):379-86. doi: 10.1042/bj2180379.
3
Reversible sensitization and desensitization of carnitine palmitoyltransferase I to inhibition by malonyl-CoA in isolated rat liver mitochondria. Significance for the mechanism of malonyl-CoA-induced sensitization.
Biochem J. 1983 Sep 15;214(3):1027-30. doi: 10.1042/bj2141027.
4
Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA.
Biochem J. 1984 Dec 15;224(3):1015-8. doi: 10.1042/bj2241015.
5
Binding of malonyl-CoA to isolated mitochondria. Evidence for high- and low-affinity sites in liver and heart and relationship to inhibition of carnitine palmitoyltransferase activity.
Biochem J. 1984 Sep 15;222(3):639-47. doi: 10.1042/bj2220639.
6
Changes in the ability of malonyl-CoA to inhibit carnitine palmitoyltransferase I activity and to bind to rat liver mitochondria during incubation in vitro. Differences in binding at 0 degree C and 37 degrees C with a fixed concentration of malonyl-CoA.
Biochem J. 1984 Sep 1;222(2):335-42. doi: 10.1042/bj2220335.
7
A cold-clamping technique for the rapid sampling of rat liver for studies on enzymes in separate cell fractions. Suitability for the study of enzymes regulated by reversible phosphorylation-dephosphorylation.
Biochem J. 1984 Jun 15;220(3):733-8. doi: 10.1042/bj2200733.
8
Altered release of carnitine palmitoyltransferase activity by digitonin from liver mitochondria of rats in different physiological states.
Biochem J. 1985 Sep 1;230(2):389-94. doi: 10.1042/bj2300389.
9
Effects of the mode of addition of acyl-CoA on the initial rate of formation of acylcarnitine in the presence of carnitine by intact rat liver mitochondria in vitro.
Biochem J. 1985 Jul 1;229(1):273-5. doi: 10.1042/bj2290273.
10
Oxidative metabolism of long-chain fatty acids in mitochondria from sheep and rat liver. Evidence that sheep conserve linoleate by limiting its oxidation.
Biochem J. 1985 Jan 1;225(1):233-7. doi: 10.1042/bj2250233.
本文引用的文献
1
Importance of experimental conditions in evaluating the malonyl-CoA sensitivity of liver carnitine acyltransferase. Studies with fed and starved rats.
Biochem J. 1981 Nov 15;200(2):217-23. doi: 10.1042/bj2000217.
2
Regulation of hepatic fatty acid metabolism. The activities of mitochondrial and microsomal acyl-CoA:sn-glycerol 3-phosphate O-acyltransferase and the concentrations of malonyl-CoA, non-esterified and esterified carnitine, glycerol 3-phosphate, ketone bodies and long-chain acyl-CoA esters in livers of fed or starved pregnant, lactating and weaned rats.
Biochem J. 1981 Jul 15;198(1):75-83. doi: 10.1042/bj1980075.
3
Effects of fasting and malonyl CoA on the kinetics of carnitine palmitoyltransferase and carnitine octanoyltransferase in intact rat liver mitochondria.
FEBS Lett. 1981 Sep 28;132(2):166-8. doi: 10.1016/0014-5793(81)81152-0.
4
Sensitivity of carnitine acyltransferase I to malonly-CoA inhibition in isolated rat liver mitochondria is quantitatively related to hepatic malonyl-CoA concentration in vivo.
Biochem J. 1982 Jul 15;206(1):177-9. doi: 10.1042/bj2060177.
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