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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Purification and peptidase activity of a bacteriolytic extracellular enzyme from Pseudomonas aeruginosa.

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.[1]

References

  1. Purification and peptidase activity of a bacteriolytic extracellular enzyme from Pseudomonas aeruginosa. Brito, N., Falcón, M.A., Carnicero, A., Gutiérrez-Navarro, A.M., Mansito, T.B. Res. Microbiol. (1989) [Pubmed]
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