| Literature DB >> 2508200 |
N Brito1, M A Falcón, A Carnicero, A M Gutiérrez-Navarro, T B Mansito.
Abstract
A bacteriolytic enzyme excreted by Pseudomonas aeruginosa Paks I was purified: samples were found to be homogeneous by gel filtration chromatography, ion exchange chromatography using CM-cellulose, immunoelectrophoresis, PAGE and SDS-PAGE. The molecular weight of the lytic enzyme was estimated to be 15,000-19,000. The enzyme was active on Gram-positive bacteria with glycine-containing interpeptide bridges in their murein layers. In addition, this lytic enzyme showed peptidase activity catalysing the hydrolysis of pentaglycine peptides into tri- and diglycine peptides.Entities:
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Year: 1989 PMID： 2508200 DOI： 10.1016/0923-2508(89)90046-6
Source DB: PubMed Journal: Res Microbiol ISSN： 0923-2508 Impact factor: 3.992