PMID: 2508200Feb 1, 1989Paper

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

Research in Microbiology
N BritoT 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.

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Citations

Oct 19, 2012·Applied Microbiology and Biotechnology·Piotr SzwedaSlawomir Milewski
Sep 29, 2011·Graefe's Archive for Clinical and Experimental Ophthalmology = Albrecht Von Graefes Archiv Für Klinische Und Experimentelle Ophthalmologie·Irina S BarequetEfrat Kessler
Dec 1, 1994·The Journal of Applied Bacteriology·C Chapuis, J P Flandrois
Apr 24, 2004·Antimicrobial Agents and Chemotherapy·Irina S BarequetEfrat Kessler
Oct 20, 2005·Journal of Bioscience and Bioengineering·Kashfia AhmedFumio Sakiyama
Nov 10, 2007·Environmental Microbiology·Christiane GoerkeBarbara C Kahl
Aug 29, 2013·Journal of the Science of Food and Agriculture·Muhammad Aqeel AshrafMuhammad Abdur Rehman
Jul 1, 1990·FEMS Microbiology Letters·A CarniceroJ M Roldán
Apr 11, 1997·The Journal of Biological Chemistry·E KesslerD E Ohman
Nov 1, 2020·Antibiotics·Alexey S AfoshinNatalia V Vasilyeva

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