Use of Monospecific Antibodies for the Purification of D-Amino Acid Oxidases from Various Sources

Abstract

D-amino acid oxidase (E.C.1.4.3.3., DAAO), a flavo-protein which catalyzes the oxidative deamination of D-amino acids, has been purified to homogeneity from hog kidney (1). The physiological role of this enzyme remains obscure, even if alternative hypotheses on its function have been proposed in recent years (2). In spite of its apparent uselessness, D-amino acid oxidase has been largely investigated as a model system for flavo-oxidases, and its kinetic parameters, physical-chemical properties, catalytic mechanism and primary structure have been determined (3,4). Unfortunately, the three-dimensional structure of the enzyme is still unknown due to the difficulty of obtaining crystals of hog enzyme suitable for X-ray studies (5). A solution to this problem would be to search for other sources of the enzyme: such a project would require much screening among various organisms and a relatively rapid purification procedure of this flavo-protein.