title: Purification of human plasma catalase and monoamine oxidase and the partial characterization of monoamine oxidase.
abstract: Human plasma catalase and monoamine oxidase were purified for the first time to homogeneity. Monoamine oxidase purified 3200-fold with the aid of DEAE-Sepharose Cl-6B and Sepharose Cl-6B chromatography was devoid of catalase, aldehyde dehydrogenase and reductase activity. Homogeneous catalase was obtained during DEAE-Sepharose C1-6B chromatography of monoamine oxidase. Monoamine oxidase was characterized physico-chemically in terms of molecular weight, electrophoretic mobility, iso-electric point, amino acid composition and specific activity. The molecular weight was estimated to be 234.5 K by exclusion chromatography and with iso-electric focusing the pI was estimated to be 5.6.
mesh_terms: D000596:Amino Acids / Q000032:analysis; D002374:Catalase / Q000097:blood*; D002847:Chromatography, Agarose; D002852:Chromatography, Ion Exchange; D006801:Humans; D007526:Isoelectric Point; D008970:Molecular Weight; D008995:Monoamine Oxidase / Q000097:blood*
chemical_list: D000596:Amino Acids; D002374:Catalase; D008995:Monoamine Oxidase