Purification of human plasma catalase and monoamine oxidase and the partial characterization of monoamine oxidase.
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.
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*
D000596:Amino Acids; D002374:Catalase; D008995:Monoamine Oxidase