SUBCELLULAR-DISTRIBUTION AND CHARACTERISTICS OF CIPROFIBROYL-COA SYNTHETASE IN RAT-LIVER - ITS POSSIBLE IDENTITY WITH LONG-CHAIN ACYL-COA SYNTHETASE

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dc.contributor.authorAMIGO, L
dc.contributor.authorMCELROY, MC
dc.contributor.authorMORALES, MN
dc.contributor.authorBRONFMAN, M
dc.date.accessioned2025-01-23T19:22:08Z
dc.date.available2025-01-23T19:22:08Z
dc.date.issued1992
dc.description.abstractThe subcellular distribution and characteristics of ciprofibroyl-CoA synthetase were studied in rat liver and compared with those of long-chain acyl-CoA synthetase (palmitate as substrate) which, as already known, is distributed among mitochondria, microsomes and peroxisomes. Upon differential centrifugation, the subcellular distribution of ciprofibroyl-CoA synthetase followed closely that of palmitoyl-CoA synthetase and was specifically inactivated in the mitochondrial fraction by freezing and thawing, a behaviour already described for palmitoyl-CoA synthetase. Both enzyme activities were found to co-purify through several steps from rat liver microsomes. By using a partially purified enzyme, the activation of ciprofibrate to its acyl-CoA ester followed Michaelis-Menten kinetics with an apparent K(m) of 0.63 +/- 0.1 mM. Ciprofibroyl-CoA synthetase was competitively inhibited by 25 and 50-mu-M-palmitic acid. Higher concentrations of the fatty acid resulted in a mixed type of inhibition. Conversely, ciprofibrate up to 0.5 mM was found to inhibit competitively palmitoyl-CoA synthetase, whereas higher concentrations also resulted in a mixed inhibition. The highest activity of ciprofibroyl-CoA synthetase was found in fat and liver homogenates. The distribution of the enzyme in different rat tissues was similar to that of palmitoyl-CoA synthetase. The present results suggest that long-chain acyl-CoA synthetase and ciprofibroyl-CoA synthetase activities reside in identical or closely related proteins.
dc.fuente.origenWOS
dc.identifier.eissn1470-8728
dc.identifier.issn0264-6021
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/98972
dc.identifier.wosidWOS:A1992HV22300040
dc.language.isoen
dc.pagina.final287
dc.pagina.inicio283
dc.revistaBiochemical journal
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleSUBCELLULAR-DISTRIBUTION AND CHARACTERISTICS OF CIPROFIBROYL-COA SYNTHETASE IN RAT-LIVER - ITS POSSIBLE IDENTITY WITH LONG-CHAIN ACYL-COA SYNTHETASE
dc.typeartículo
dc.volumen284
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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