Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1983-6-10
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.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1287
pubmed:author
pubmed:issnType
Print
pubmed:volume
129
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
489-97
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1983
pubmed:articleTitle
A phage-associated murein hydrolase in Streptococcus pneumoniae infected with bacteriophage Dp-1.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't