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...
Tallennettuna:
| Julkaisussa: | J Bacteriol |
|---|---|
| Päätekijä: | |
| Aineistotyyppi: | Artigo |
| Kieli: | Inglês |
| Julkaistu: |
American Society for Microbiology (ASM)
1975
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| Aiheet: | |
| Linkit: | 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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