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Liver mitochondria, confirmed as intact by complete suppression of succinate uptake and oxidation, possess a carnitine palmitoyltransferase I that is totally inhibited by malonyl CoA
Journal article   Peer reviewed

Liver mitochondria, confirmed as intact by complete suppression of succinate uptake and oxidation, possess a carnitine palmitoyltransferase I that is totally inhibited by malonyl CoA

K.A.H. Abo-Hashema, M.H. Cake and I.C. Potter
Biochemical and Biophysical Research Communications, Vol.258(3), pp.778-783
1999
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Abstract

Succinate dehydrogenase activity in mitochondria, which were isolated by centrifuging partially purified mitochondria through 1.315 M sucrose, was completely suppressed when [14C]succinate uptake was abolished by prior incubation of the mitochondria with carbonyl cyanide p-trifluoromethoxyphenylhydrazone (FCCP) and valinomycin. The conclusion that these mitochondria were intact was confirmed by the fact that, when these mitochondria were broken by a freeze-thaw cycle followed by sonication, such inhibition was totally abolished. The yield of mitochondria, microsomes, and peroxisomes from the initial homogenate was 17.8, < 0.1, and 0%, respectively, indicating that the mitochondria were not only intact but also essentially free of contamination from microsomes and peroxisomes. The overt form of carnitine palmitoyltransferase (CPT I) in these intact and pure mitochondria was totally inhibited by malonyl CoA, indicating that previous reports of incomplete inhibition in mitochondrial preparations resulted from interference from CPT activity in the inner mitochondrial membrane (CPT II), microsomes, or peroxisomes.

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Citation topics
1 Clinical & Life Sciences
1.197 Molecular & Cell Biology - Mitochondria
1.197.1196 Inborn Metabolic Errors
Web Of Science research areas
Biochemistry & Molecular Biology
Biophysics
ESI research areas
Biology & Biochemistry
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