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The reaction of bovine plasma amine oxidase, a glycoprotein, with Concanavalin A in 0.1 M potassium phosphate buffer, pH 7.0 at 25 degrees C were investigated by equilibrium and kinetic methods. A tentative mechanism for the reaction was derived. The Concanavalin A-enzyme interaction was used to show that the carbohydrate is not essential for activity and that the carbohydrate is covalently attached to the protein at a site distant from the active site. Concanavalin A-Sepharose 4B affinity chromatography of the enzyme was found to be useful for obtaining the pure enzyme. Chromatographic conditions which elute the enzyme are reported. The superiority of the Concanavalin A-Sepharose 4B over that of the substrate-affinity Sepharose affinity support is discussed. The phenylhydrazone derivative of the enzyme, which was inactive, was shown to bind to the concanavalin A-Sepharose column.
H Ishizaki, and
K T Yasunobu
April 1971,
Biochimica et biophysica acta,
H Ishizaki, and
K T Yasunobu
September 1982,
Analytical biochemistry,
H Ishizaki, and
K T Yasunobu
January 1983,
Methods in enzymology,
H Ishizaki, and
K T Yasunobu
January 1982,
Methods in enzymology,
H Ishizaki, and
K T Yasunobu
January 1981,
Preparative biochemistry,
H Ishizaki, and
K T Yasunobu
July 1984,
Biochemical pharmacology,
H Ishizaki, and
K T Yasunobu
March 2006,
Bioorganic & medicinal chemistry,
H Ishizaki, and
K T Yasunobu
August 1975,
Biochimica et biophysica acta,
H Ishizaki, and
K T Yasunobu
January 1987,
The Journal of biological chemistry,
H Ishizaki, and
K T Yasunobu
May 1970,
Biochemical and biophysical research communications,
