ACYL-COA SYNTHETASE AND THE PEROXISOMAL ENZYMES OF BETA-OXIDATION IN HUMAN-LIVER - QUANTITATIVE-ANALYSIS OF THEIR SUBCELLULAR-LOCALIZATION

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dc.contributor.authorBRONFMAN, M
dc.contributor.authorINESTROSA, NC
dc.contributor.authorNERVI, FO
dc.contributor.authorLEIGHTON, F
dc.date.accessioned2025-01-23T19:43:42Z
dc.date.available2025-01-23T19:43:42Z
dc.date.issued1984
dc.description.abstractThe presence of acyl CoA synthetase (EC 6.2.1.3) in peroxisomes and the subcellular distribution of .beta.-oxidation enzymes in human liver were investigated by using a single-step fractionation method of whole liver homogenates in metrizamide continuous density gradients and a novel procedure of computer analysis of results. Peroxisomes contain 16% of the liver palmitoyl CoA synthetase activity, and 21% and 60% of the enzyme activity was localized in mitochondria and microsomal fractions, respectively. Fatty acyl CoA oxidase was localized exclusively in peroxisomes, confirming previous results. Human liver peroxisomes contribute 13%, 17% and 11% of the liver activities of crotonase, .beta.-hydroxyacyl CoA dehdyrogenase and thiolase, respectively. The absolute activities found in peroxisomes for the enzymes investigated suggest that in human liver fatty acyl CoA oxidase is the rate-limiting enzyme of the peroxisomal .beta.-oxidation pathway, when palmitic acid is the substrate.
dc.fuente.origenWOS
dc.identifier.eissn1470-8728
dc.identifier.issn0264-6021
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/99778
dc.identifier.wosidWOS:A1984TY10800004
dc.issue.numero3
dc.language.isoen
dc.pagina.final720
dc.pagina.inicio709
dc.revistaBiochemical journal
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titleACYL-COA SYNTHETASE AND THE PEROXISOMAL ENZYMES OF BETA-OXIDATION IN HUMAN-LIVER - QUANTITATIVE-ANALYSIS OF THEIR SUBCELLULAR-LOCALIZATION
dc.typeartículo
dc.volumen224
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
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