SCREENING OF BOTHROPS SNAKE-VENOMS FOR L-AMINO-ACID OXIDASE ACTIVITY

Citation
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
Citations number
26
Categorie Soggetti
Biothechnology & Applied Migrobiology",Biology
ISSN journal
02732289
Volume
51-2
Year of publication
1995
Pages
197 - 210
Database
ISI
SICI code
0273-2289(1995)51-2:<197:SOBSFL>2.0.ZU;2-1
Abstract
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.