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Purification of bovine plasma amine oxidase

✍ Scribed by P. Turini; S. Sabatini; O. Befani; F. Chimenti; C. Casanova; P.L. Riccio; B. Mondovi

Publisher
Elsevier Science
Year
1982
Tongue
English
Weight
349 KB
Volume
125
Category
Article
ISSN
0003-2697

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✦ Synopsis

A new method for the purification of bovine plasma amine oxidase is described. The enzyme is purified by ammonium sulfate precipitation and by affinity chromatography performed with AH-Sepharose 4B and concanavalin A-Sepharose. Three activity peaks were separated, all showing similar properties. Specific activity is the highest described for this enzyme. The enzyme appears to contain 2 copper atoms and 1 carbonyl group/molecule.

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