PURIFICATION OF THE PEROXISOMAL FATTY ACYL-COA OXIDASE FROM RAT-LIVER

Simple item page
dc.contributor.authorINESTROSA, NC
dc.contributor.authorBRONFMAN, M
dc.contributor.authorLEIGHTON, F
dc.date.accessioned2025-01-23T19:44:29Z
dc.date.available2025-01-23T19:44:29Z
dc.date.issued1980
dc.description.abstractFatty acyl-CoA oxidase, the rate limiting enzyme of the peroxisomal fatty acid oxidizing system, was purified from rat liver to near homogeneity by a procedure involving affinity chromatography of its apoenzyme on FAD-Sepharose. The oxidase presents an absolute requirement for the dinucleotide which is weakly bound to the apoenzyme (KD, 0.6 .mu.M). The highest specific activity obtained was 27 units/mg protein. The purified enzyme was 2 major polypeptides with apparent MW of 45,000 and 22,000. The enzyme is a flavoprotein with non-covalently bound flavin adenin dinucleotide composed of 4 subunits, 2 of 45,000 MW and 2 of 22,000 MW.
dc.fuente.origenWOS
dc.identifier.eissn1090-2104
dc.identifier.issn0006-291X
dc.identifier.urihttps://repositorio.uc.cl/handle/11534/100055
dc.identifier.wosidWOS:A1980KB03200002
dc.issue.numero1
dc.language.isoen
dc.pagina.final12
dc.pagina.inicio7
dc.revistaBiochemical and biophysical research communications
dc.rightsacceso restringido
dc.subject.ods03 Good Health and Well-being
dc.subject.odspa03 Salud y bienestar
dc.titlePURIFICATION OF THE PEROXISOMAL FATTY ACYL-COA OXIDASE FROM RAT-LIVER
dc.typeartículo
dc.volumen95
sipa.indexWOS
sipa.trazabilidadWOS;2025-01-12
Files
Collections
Artículos de revistas