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Purification and properties of a serine protease from Pseudomonas matophilia.

The extracellular protease of Pseudomonas maltophilia was partially purified by ammonium sulfate precipitation and chromatography on Sephadex G-75 and Bio-rex 70. Gel electrophoresis revealed minor impurities. The enzyme exhibited the following properties: (i) molecular weight, 35,000; (ii) A see ar...

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Detalles Bibliográficos
Publicado en:J Bacteriol
Autor Principal: Boethling, R S
Formato: Artigo
Idioma:Inglês
Publicado: American Society for Microbiology (ASM) 1975
Assuntos:
Acceso en liña:https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC246021/
https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/234950/
https://ncbi.nlm.nih.govhttps://doi.org/10.1128/jb.121.3.933-941.1975
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