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.
Brito
N
N
Departamento de Microbiología y Biología Celular, Facultad de Biología, Universidad de La Laguna, Tenerife, Spain.
Falcón
M A
MA
Carnicero
A
A
Gutiérrez-Navarro
A M
AM
Mansito
T B
TB
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
D010447:Peptide Hydrolases