Gelatinase activity in mycobacterium bovis protein extract
Int. j. lepr. other mycobact. dis
; 70(4): 260-268, Dec., 2002. ilus, tab, graf
Article
em En
| SES-SP, HANSEN, HANSENIASE, SESSP-ILSLACERVO, SES-SP
| ID: biblio-1227122
Biblioteca responsável:
BR191.1
Localização: [{"text": "BR191.1"}]
ABSTRACT
Proteases are well-recognized as virulence factors in different pathologies, resulting in tissue damage potential. Despite efforts over the past few years to identify mycobacterial protein antigens, there is little information regarding the role of mycobacterial proteinase activities. In this study, by zymography techniques, we have detected and partially studied some biochemical properties of Mycobacterium bovis proteases, such as pH dependency of activity and susceptibility to classical proteinase inhibitors. We observed optimal proteolytic activity at pH 8. Some proteinases were inhibited by classic inhibitors of serine proteases, such as PMSF, AEBSF, and 3-4 DCI. In some AEBSF pre-treated preparations we observed residual gelatinase activity in Rf 0.32. This gelatinase was stimulated by Zn2+ and inhibited by OPA (1 mM). This last effect was reversed by exposure to equimolar quantitative OPA/Zn+2 (1 mM/1 mM). These results suggest the existence of serine proteinase and metalloproteinase types in protein extracts of Mycobacterium bovis.
Texto completo:
1
Coleções:
06-national
/
BR
Base de dados:
HANSEN
/
HANSENIASE
/
SES-SP
/
SESSP-ILSLACERVO
Assunto principal:
Gelatinases
/
Mycobacterium bovis
Tipo de estudo:
Prognostic_studies
Idioma:
En
Revista:
Int. j. lepr. other mycobact. dis
Ano de publicação:
2002
Tipo de documento:
Article