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. 1985 Jul 1;229(1):273–275. doi: 10.1042/bj2290273

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.

V A Zammit
PMCID: PMC1145178  PMID: 4038262

Abstract

Time courses for the formation of palmitoylcarnitine from palmitoyl-CoA and carnitine, catalysed by the overt activity of carnitine palmitoyltransferase (CPT I) in rat liver mitochondria, were obtained. Significant initial non-linearity was observed only when reactions were started by addition of a concentrated solution of palmitoyl-CoA (4mM, to give a final concentration of 100 microM) uncomplexed to albumin. Minimal effects were observed when the reactions were started by addition of palmitoyl-CoA-albumin mixtures, even though the final palmitoyl-CoA/albumin molar ratios in the assay medium were identical in the two sets of experiments.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Bremer J., Woldegiorgis G., Schalinske K., Shrago E. Carnitine palmitoyltransferase. Activation by palmitoyl-CoA and inactivation by malonyl-CoA. Biochim Biophys Acta. 1985 Jan 9;833(1):9–16. doi: 10.1016/0005-2760(85)90247-4. [DOI] [PubMed] [Google Scholar]
  2. Cook G. A. Involvement of hysteretic effects in the inhibition of carnitine palmitoyltransferase by malonyl-CoA. Biochem J. 1984 Dec 15;224(3):1015–1018. doi: 10.1042/bj2241015. [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Cook G. A., Otto D. A., Cornell N. W. Malonyl-CoA inhibition of carnitine palmitoyltransferase: interpretation of I50 and K1 values. Biochem J. 1983 May 15;212(2):525–527. doi: 10.1042/bj2120525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  4. McCormick K., Notar-Francesco V. J. Importance of albumin binding in the assay for carnitine palmitoyltransferase. Biochem J. 1983 Nov 15;216(2):495–498. doi: 10.1042/bj2160495. [DOI] [PMC free article] [PubMed] [Google Scholar]
  5. McGarry J. D., Foster D. W. 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):217–223. doi: 10.1042/bj2000217. [DOI] [PMC free article] [PubMed] [Google Scholar]
  7. Robinson I. N., Zammit V. A. 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):177–179. doi: 10.1042/bj2060177. [DOI] [PMC free article] [PubMed] [Google Scholar]
  8. Saggerson E. D. Does fasting decrease the inhibitory effect of malonyl-CoA on hepatic beta-oxidation? Biochem J. 1982 Nov 15;208(2):525–528. doi: 10.1042/bj2080525. [DOI] [PMC free article] [PubMed] [Google Scholar]
  9. Zammit V. A., Corstorphine C. G., Gray S. R. 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):335–342. doi: 10.1042/bj2220335. [DOI] [PMC free article] [PubMed] [Google Scholar]
  10. Zammit V. A. 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):953–956. doi: 10.1042/bj2100953. [DOI] [PMC free article] [PubMed] [Google Scholar]
  11. Zammit V. A. 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):1027–1030. doi: 10.1042/bj2141027. [DOI] [PMC free article] [PubMed] [Google Scholar]
  12. Zammit V. A. The effect of glucagon treatment and starvation of virgin and lactating rats on the rates of oxidation of octanoyl-L-carnitine and octanoate by isolated liver mitochondria. Biochem J. 1980 Aug 15;190(2):293–300. doi: 10.1042/bj1900293. [DOI] [PMC free article] [PubMed] [Google Scholar]
  13. Zammit V. A. 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):379–386. doi: 10.1042/bj2180379. [DOI] [PMC free article] [PubMed] [Google Scholar]

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