l-Amino acid oxidase from Vipera palaestinae venom: Purification and assay

Nurit Shaham, Avner Bdolah

Research output: Contribution to journalArticlepeer-review


1. 1. 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. 2. 2. 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. 3. 3. 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. 4. 4. 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,IN3-IN4,697-698
JournalComparative Biochemistry and Physiology - B Biochemistry and Molecular Biology
Issue number4
StatePublished - 15 Dec 1973


  • Vipera palaestinae
  • l-Amino oxidase
  • venom


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