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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1983-6-10
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pubmed:abstractText |
A phage-associated murein hydrolase activity capable of degrading pneumococcal cell walls was isolated and purified to homogeneity from the phage-induced lysate of an autolysis-defective pneumococcal mutant infected with the bacteriophage Dp-1. Some properties of the enzyme resembled those of the wild-type (host) pneumococcal murein hydrolase: cell walls prepared from ethanolamine-grown pneumococci were resistant to the enzyme; the activity was inhibited by the Forssman antigen and was sensitive to proteolytic enzymes. The phage-associated enzyme was not inhibited by antiserum prepared against the purified pneumococcal murein hydrolase; the activity was stimulated by reducing agents and was partially inhibited by cardiolipin. The subunit molecular weight of the phage-associated enzyme was somewhat smaller (31 000) than that of the pneumococcal hydrolase (35 000). This appears to be the first description of a phage-associated murein hydrolase activity in pneumococci.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0022-1287
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
129
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
489-97
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:6132961-Amidohydrolases,
pubmed-meshheading:6132961-Bacteriolysis,
pubmed-meshheading:6132961-Bacteriophages,
pubmed-meshheading:6132961-Cell Wall,
pubmed-meshheading:6132961-Chromatography, Gel,
pubmed-meshheading:6132961-Hydrogen-Ion Concentration,
pubmed-meshheading:6132961-Molecular Weight,
pubmed-meshheading:6132961-Mutation,
pubmed-meshheading:6132961-N-Acetylmuramoyl-L-alanine Amidase,
pubmed-meshheading:6132961-Streptococcus pneumoniae,
pubmed-meshheading:6132961-Temperature
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pubmed:year |
1983
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pubmed:articleTitle |
A phage-associated murein hydrolase in Streptococcus pneumoniae infected with bacteriophage Dp-1.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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