Carnitine palmitoyltransferase located in the erythrocyte plasma membrane is sensitive to inhibition by malonyl-CoA and 2-bromopalmitoyl-CoA plus carnitine. Although this inhibition and other properties suggest similarities to the intracellular enzymes in other tissues, no cross-reaction was observed with antisera to the peroxisomal or to the mitochondrial inner-membrane enzyme. The activity was solubilized by and was stable in Triton X-100, which destroys the enzymes found in microsomes and in the mitochondrial outer membrane. The substrate specificity is broader than for the intracellular enzymes, the activities with stearoyl-CoA (114%) and arachidonoyl-CoA (97%) being equal to that with palmitoyl-CoA, and the activities with linoleoyl-CoA (44%) and erucoyl-CoA (46%) about half that with palmitoyl-CoA. The function of this carnitine palmitoyltransferase is probably to buffer the acyl-CoA present in the erythrocyte for turnover of the fatty acyl groups of the membrane lipids.
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May 1991
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Research Article|
May 01 1991
Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity Available to Purchase
R R Ramsay;
R R Ramsay
*Department of Biochemistry and Biophysics, University of California, San Francisco, and Molecular Biology Division, Veterans Administration Medical Center, San Francisco, CA 94121, U.S.A.
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G Mancinelli;
G Mancinelli
†Istituto di Scienze Biochimiche, Università degli Studi ‘G. D'Annunzio’, 66100 Chieti, Italy.
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A Arduini
A Arduini
†Istituto di Scienze Biochimiche, Università degli Studi ‘G. D'Annunzio’, 66100 Chieti, Italy.
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Publisher: Portland Press Ltd
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© 1991 The Biochemical Society, London
1991
Biochem J (1991) 275 (3): 685–688.
Citation
R R Ramsay, G Mancinelli, A Arduini; Carnitine palmitoyltransferase in human erythrocyte membrane. Properties and malonyl-CoA sensitivity. Biochem J 1 May 1991; 275 (3): 685–688. doi: https://doi.org/10.1042/bj2750685
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