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.

journal_name

Res Microbiol

journal_title

Research in microbiology

authors

Brito N,Falcón MA,Carnicero A,Gutiérrez-Navarro AM,Mansito TB

doi

10.1016/0923-2508(89)90046-6

subject

Has Abstract

pub_date

1989-02-01 00:00:00

pages

125-37

issue

2

eissn

0923-2508

issn

1769-7123

pii

0923-2508(89)90046-6

journal_volume

140

pub_type

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