Isolation and characterization of renin-like aspartic-proteases from Echis ocellatus venom.
Toxicon
; 137: 92-94, 2017 Oct.
Article
en En
| MEDLINE
| ID: mdl-28734982
ABSTRACT
Three aspartic proteases (SVAPs) have been isolated from venom of the saw-scaled viper, Echis ocellatus. In confirmation of prior transcriptomic predictions, all three forms match to sequences of either of the two SVAP transcripts (EOC00051 and EOC00123), have a molecular weight of 42 kDa and possess a single N-glycan. The SVAPs act in a renin-like manner, specifically cleaving human and porcine angiotensinogen into angiotensin-1 and possess no general protease activity. Their activity is completely inhibited by the aspartyl protease inhibitor Pepstatin A.
Palabras clave
Texto completo:
1
Colección:
01-internacional
Banco de datos:
MEDLINE
Asunto principal:
Venenos de Víboras
/
Angiotensina I
/
Angiotensinógeno
/
Viperidae
/
Proteasas de Ácido Aspártico
Límite:
Animals
/
Humans
Idioma:
En
Revista:
Toxicon
Año:
2017
Tipo del documento:
Article