PURIFICATION AND PROPERTIES OF THE L-AMINO-ACID OXIDASE FROM MALAYAN PIT VIPER (CALLOSELASMA-RHODOSTOMA) VENOM

The L-amino acid oxidase of Malayan pit viper (Calloselasma rhodostoma ) venom was purified to electrophoretic homogeneity. The molecular wei ght of the enzyme was 132,000 as determined by Sephadex G-200 gel filt ration chromatography and 66,000 as determined by sodium dodecyl sulfa te-polyacrylamide gel electrophoresis. It is a glycoprotein, has an is oelectric point of 4.4, and contains 2 mol of flavin mononucleotide pe r mole of enzyme. The N-terminal amino acid sequence of the enzyme was A-D-D-R-N-P-L-A-E-E-F-Q-E-N-N-Y-E-E-F-L. Kinetic studies suggest the presence of a alkyl side-chain binding site in the enzyme and that the binding site comprises at least four hydrophobic subsites. The charac teristics of the binding site differ slightly from those of cobra veno m L-amino acid oxidases. (C) 1994 Academic Press, Inc.