Heterogeneity of human liver alanine aminotransferase due to sulfhydryl groups oxidation.
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.
Gubern
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Departament de Bioquimica i Fisiologia, Facultat de Química, Universitat de Barcelona, Spain.
Imperial
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Busquets
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Cortés
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A
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
D007527:Isoenzymes; D013438:Sulfhydryl Compounds; D008623:Mercaptoethanol; D000410:Alanine Transaminase