Screening ofBothrops snake venoms forl-amino acid oxidase activity View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1995-09

AUTHORS

Marcos L. Pessatti, José D. Fontana, Maria F. D. Furtado, Manoel F. Guimãraes, Lorenzo R. S. Zanette, Walliana T. Costa, Madalena Baron

ABSTRACT

Toxins, enzymes, and biologically active peptides are the main components of snake venoms from the genus Bothrops. Following the venom inoculation, the local effects are hemorrhage, edema, and myonecrosis. Nineteen 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 acid oxidase (LAO) activity was also characterized. Flavin adenine dinucleotide (FAD) is its associate coenzyme. B. cotiara venom LAO catalyzed the oxidative deamination of several L-amino acids, and the best substrates were methionine, leucine, tryptophan, and phenylalanine, hence, its potential application for the use of biosensors for aspartame determination and for the removal of amino acids from plasma. High levels for LAO were also found in other species than B. cotiara. In addition, the technique of isoelectric focusing (IEF) was employed as a powerful tool to study the iso- or multi-enzyme distribution for LAO activity in the B. cotiara snake venom. More... »

PAGES

197-210

References to SciGraph publications

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/bf02933424

DOI

http://dx.doi.org/10.1007/bf02933424

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1030314737

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7668847


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