Isolation and characterization of an unusual form of L-amino acid oxidase from King cobra (Ophiophagus hannah) venom.
The L-amino acid oxidase (EC 1. 4. 3. 2) from King cobra (Ophiophagus hannah) venom was purified to electrophoretic homogeneity. The molecular weight of the enzyme was determined to be 140000 when examined by gel filtration and 68000 by SDS-polyacrylamide gel electrophoresis. The enzyme had an isoelectric point of 4.5 and an intravenous LD50 of 5 micrograms/g in mice. It is a glycoprotein and contains two moles of FAD per mole of enzyme. The enzyme exhibited unusual thermal stability and unlike most other venom L-amino acid oxidases, it was stable in alkaline solution and was not inactivated by freezing.
Tan
N H
NH
Department of Biochemistry, University of Malaya, Kuala Lumpur, Malaysia.
Saifuddin
M N
MN
D000594:Amino Acid Oxidoreductases / Q000032:analysis*; D000818:Animals; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004546:Elapid Venoms / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability; D050830:L-Amino Acid Oxidase
D004546:Elapid Venoms; D000594:Amino Acid Oxidoreductases; D050830:L-Amino Acid Oxidase