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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.
M M Oosthuizen, and
B van Wyk, and
J C Schabort
May 1996,
Protein expression and purification,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
February 1986,
Planta,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
May 1965,
The Journal of biological chemistry,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
May 1962,
The Journal of biological chemistry,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
April 1962,
Biochimica et biophysica acta,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
October 1966,
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M M Oosthuizen, and
B van Wyk, and
J C Schabort
January 1977,
The Biochemical journal,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
July 1992,
Biochimica et biophysica acta,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
January 1963,
Voprosy meditsinskoi khimii,
M M Oosthuizen, and
B van Wyk, and
J C Schabort
August 1986,
Biochemical medicine and metabolic biology,
