Purification and properties of an inducible cephalosporinase from Pseudomonas maltophilia GN12873.

An inducible cephalosporinase was purified from Pseudomonas maltophilia GN12873. The pI was 8.4, and the molecular weight was ca. 56,000 by gel filtration or 27,000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, suggesting that this enzyme had two subunits. The optimal pH and optimal...

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Vydáno v:	Antimicrob Agents Chemother
Hlavní autoři:	Saino, Y, Inoue, M, Mitsuhashi, S
Médium:	Artigo
Jazyk:	Inglês
Vydáno:	American Society for Microbiology (ASM) 1984
Témata:	Research Article
On-line přístup:	https://ncbi.nlm.nih.govhttps://pmc.ncbi.nlm.nih.gov/articles/PMC185518/ https://ncbi.nlm.nih.govhttps://pubmed.ncbi.nlm.nih.gov/6609682/ https://ncbi.nlm.nih.govhttps://doi.org/10.1128/aac.25.3.362
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