L amino acid oxidase from Vipera palaestinae venom: Purification and assay

N. Shaham, A. Bdolah

Research output: Contribution to journalArticlepeer-review

Abstract

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.

Original languageEnglish
Pages (from-to)691-696
Number of pages6
JournalComparative Biochemistry and Physiology
Volume46
Issue number4 B
StatePublished - 1973

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