L Amino acid oxidase was isolated from the venom of Vipera palaestinae by a procedure involving heat treatment, ammonium sulfate precipitation, gel filtration, adsorption on calcium phosphate gel and chromatography on DEAE cellulose. The enzyme was homogeneous in the ultracentrifuge and had a molecular weight of approximately 130,000. The pure enzyme showed on acrylamide electrophoresis at least three bands with enzymic activity. L Amino acid oxidase was assayed with L leucine as a substrate and phenol indo 2:6 dichlorophenol as an electron acceptor. This assay was compared to another one using L kynurenine as a substrate. Optimal conditions for storage of the enzyme were found to be either at -15°C with 0.2 M acetate or under nitrogen at 0°C.
|Number of pages||6|
|Journal||Comparative Biochemistry and Physiology|
|Issue number||4 B|
|State||Published - 1973|