Identification and properties of two extracellular proteases from Brevundimonas diminuta
Braz. j. microbiol
; 31(1): 25-29, jan.-mar. 2000. ilus, tab
Artigo
em Inglês
| LILACS
| ID: lil-306361
Biblioteca responsável:
BR32.1
RESUMO
Extracellular proteases from Brevundimonas diminuta (syn. Pseudomonas diminuta) were studied in sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE) containing a copolymerized substrate. Two proteases were detected migrating at 67kDa and 50 kDa both of them hydrolysed preferentially gelatin, but casein was also degraded and a slight hydrolysis was observed with hemoglobin. No detectable extracellular proteolytic activity was found in bovine serum albumin-containing gels. The optima temperature and pH for proteolytic activity were between 40ºC and 50ºC in a pH ranging from 7.0 to 11.0, respectively. These enzymes were isolated by analytical high performance liquid chromatography (HPLC). Proteases assays with the synthetic substrate Z-Phe-Arg-MCA and inhibitors EGTA, EDTA and 1, 10 phenanthroline point out that these enzymes are metalloproteases.
Texto completo:
Disponível
Coleções:
Bases de dados internacionais
Base de dados:
LILACS
Assunto principal:
Pseudomonadaceae
/
Pseudomonas
/
Técnicas In Vitro
/
Metaloendopeptidases
/
Eletroforese em Gel de Poliacrilamida
/
Enzimas
Tipo de estudo:
Estudo diagnóstico
/
Estudo prognóstico
Limite:
Animais
Idioma:
Inglês
Revista:
Braz. j. microbiol
Assunto da revista:
Microbiologia
Ano de publicação:
2000
Tipo de documento:
Artigo
País de afiliação:
Brasil
Instituição/País de afiliação:
Fundação Instituto Oswaldo Cruz/BR
/
Universidade Federal do Rio de Janeiro/BR