Ml. Pessatti et al., SCREENING OF BOTHROPS SNAKE-VENOMS FOR L-AMINO-ACID OXIDASE ACTIVITY, Applied biochemistry and biotechnology, 51-2, 1995, pp. 197-210
Toxins, enzymes, and biologically active peptides are the main compone
nts of snake venoms from the genus Bothrops. Following the venom inocu
lation, the local effects are hemorrhage, edema, and myonecrosis. Nine
teen different species of Brazilian Bothrops were screened for protein
content and L-amino acid oxidase activity. B. cotiara, formerly found
in the South of Brazil, is now threatened with extinction. Its venom
contains a highly hemorrhagic fraction and, as expected from the deep
yellow color of the corresponding lyophilized powder, a high L-amino a
cid oxidase (LAO) activity was also characterized. Flavin adenine dinu
cleotide (FAD) is its associate coenzyme. B. cotiara venom LAO catalyz
ed the oxidative deamination of several L-amino acids, and the best su
bstrates were methionine, leucine, tryptophan, and phenylalanine, henc
e, its potential application for the use in biosensors for aspartame d
etermination and for the removal of amino acids from plasma. High leve
ls for LAO were also found in other species than B. cotiara. In additi
on, the technique of isoelectric focusing (IEF) was employed as a powe
rful tool to study the iso- or multienzyme distribution for LAO activi
ty in the B. cotiara snake venom.