Identification and properties of two extracellular proteases from Brevundimonas diminuta
Braz. j. microbiol
;
31(1): 25-29, jan.-mar. 2000. ilus, tab
Artículo
en Inglés
| LILACS
| ID: lil-306361
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:
Disponible
Índice:
LILACS (Américas)
Asunto principal:
Pseudomonadaceae
/
Pseudomonas
/
Técnicas In Vitro
/
Metaloendopeptidasas
/
Electroforesis en Gel de Poliacrilamida
/
Enzimas
Tipo de estudio:
Estudio diagnóstico
/
Estudio pronóstico
Límite:
Animales
Idioma:
Inglés
Revista:
Braz. j. microbiol
Asunto de la revista:
Microbiologia
Año:
2000
Tipo del documento:
Artículo
País de afiliación:
Brasil
Institución/País de afiliación:
Fundação Instituto Oswaldo Cruz/BR
/
Universidade Federal do Rio de Janeiro/BR
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