| Literature DB >> 3298686 |
J L García, E García, A Arrarás, P García, C Ronda, R López.
Abstract
Cp-1, a small virulent bacteriophage infecting Streptococcus pneumoniae, encodes its own lytic enzyme (CPL). A fragment of Cp-1 DNA containing the gene cpl coding for CPL was cloned and expressed in high amounts in Escherichia coli. CPL was purified to electrophoretic homogeneity by using affinity chromatography on choline-Sepharose (T. Briese and R. Hakenbeck, Eur. J. Biochem. 146:417-427, 1985), and the enzyme showing a Mr of 39,000 was characterized as a muramidase. This muramidase required for in vivo and in vitro activity the presence of choline in the teichoic acids of the pneumococcal cell walls. Free choline or lipoteichoic acid noncompetitively inhibited the activity of CPL.Entities:
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Year: 1987 PMID: 3298686 PMCID: PMC255702 DOI: 10.1128/JVI.61.8.2573-2580.1987
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103