L-Amino acid oxidase from Naja naja oxiana venom.
Comp Biochem Physiol B Biochem Mol Biol
; 149(4): 572-80, 2008 Apr.
Article
en En
| MEDLINE
| ID: mdl-18294891
A new l-amino acid oxidase (LAAO) was isolated from the Central Asian cobra Naja naja oxiana venom by size exclusion, ion exchange and hydrophobic chromatography. The N-terminal sequence and the internal peptide sequences share high similarity with other snake venom l-amino acid oxidases, especially with those isolated from elapid venoms. The enzyme is stable at low temperatures (-20 degrees C, -70 degrees C) and loses its activity by heating at 70 degrees C. Specific substrates for the isolated protein are l-phenylalanine, l-tryptophan, l-methionine and l-leucine. The enzyme has antibacterial activity inhibiting the growth of Gram-positive (Bacillus subtilis) and Gram-negative (Escherichia coli) bacteria. N. naja oxiana LAAO dose-dependently inhibited ADP- or collagen-induced platelet aggregation with IC(50) of 0.094 microM and 0.036 microM, respectively. The antibacterial and anti-aggregating activity was abolished by catalase.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Elapidae
/
Venenos Elapídicos
/
Aminoácido Oxidorreductasas
Límite:
Animals
Idioma:
En
Revista:
Comp Biochem Physiol B Biochem Mol Biol
Asunto de la revista:
BIOLOGIA MOLECULAR
/
BIOQUIMICA
Año:
2008
Tipo del documento:
Article
País de afiliación:
Estonia
Pais de publicación:
Reino Unido