title: Heterogeneity of human liver alanine aminotransferase due to sulfhydryl groups oxidation.
abstract: The cytosolic isoenzyme of human liver alanine aminotransferase exhibited a progressive change in its chromatographic behavior on DEAE-Sepharose when partially purified preparations were stored for up to 8 days at 4 degrees C. This change was characterized by the appearance of an additional chromatographic variant and was avoided by addition of 2-mercaptoethanol. The experimental evidence presented indicates that the progressive oxidation of free sulfhydryl groups of the enzyme is responsible for the charge modifications and heterogeneity observed.
authors.affiliation: Departament de Bioquimica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
authors.forename: G
authors.initials: G
authors.lastname: Gubern
authors.forename: S
authors.initials: S
authors.lastname: Imperial
authors.forename: M
authors.initials: M
authors.lastname: Busquets
authors.forename: A
authors.initials: A
authors.lastname: Cortés
mesh_terms: D000410:Alanine Transaminase / Q000302:isolation & purification / Q000378:metabolism*; D002852:Chromatography, Ion Exchange; D003600:Cytosol / Q000201:enzymology; D006801:Humans; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000201:enzymology*; D008623:Mercaptoethanol / Q000494:pharmacology*; D010084:Oxidation-Reduction; D013438:Sulfhydryl Compounds / Q000378:metabolism
chemical_list: D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D008623:Mercaptoethanol; D000410:Alanine Transaminase