title: Purification and peptidase activity of a bacteriolytic extracellular enzyme from Pseudomonas aeruginosa.
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.
authors.affiliation: Departamento de Microbiología y Biología Celular, Facultad de Biología, Universidad de La Laguna, Tenerife, Spain.
authors.forename: N
authors.initials: N
authors.lastname: Brito
authors.forename: M A
authors.initials: MA
authors.lastname: Falcón
authors.forename: A
authors.initials: A
authors.lastname: Carnicero
authors.forename: A M
authors.initials: AM
authors.lastname: Gutiérrez-Navarro
authors.forename: T B
authors.initials: TB
authors.lastname: Mansito
mesh_terms: D001433:Bacteriolysis; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D007122:Immunoelectrophoresis; D008970:Molecular Weight; D009391:Nephelometry and Turbidimetry; D010447:Peptide Hydrolases / Q000302:isolation & purification / Q000502:physiology; D011550:Pseudomonas aeruginosa / Q000201:enzymology*; D013211:Staphylococcus aureus / Q000187:drug effects / Q000254:growth & development
chemical_list: D010447:Peptide Hydrolases