Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
2
|
| pubmed:dateCreated |
1980-6-25
|
| pubmed:abstractText |
Clostridium perfringens and isolated walls of this organism autolysed rapidly when incubated in buffer at pH 7.0 with the release of free-reducing groups but no N-terminal amino acids. The predominant autolytic enzyme was an endo-beta-N-acetylglucosaminidase, and an endo-beta-N-acetylmuramidase was also present. The autolytic enzymes could be solubilized by extraction of the organisms with 5 M-LiCl and would then subsequently bind to and rapidly lyse walls of Micrococcus luteus and, more slowly, formamide-extracted walls of C. perfringens and walls of Bacillus subtilis. Lysis of C. perfringens walls by these extracted enzymes could not be demonstrated.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical | |
| pubmed:status |
MEDLINE
|
| pubmed:month |
Oct
|
| pubmed:issn |
0022-1287
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:volume |
114
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
349-54
|
| pubmed:dateRevised |
2007-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:44314-Acetylglucosaminidase,
pubmed-meshheading:44314-Cell Wall,
pubmed-meshheading:44314-Clostridium perfringens,
pubmed-meshheading:44314-Glycoside Hydrolases,
pubmed-meshheading:44314-Hydrogen-Ion Concentration,
pubmed-meshheading:44314-Hydrolysis,
pubmed-meshheading:44314-Muramidase,
pubmed-meshheading:44314-Polysaccharides
|
| pubmed:year |
1979
|
| pubmed:articleTitle |
Characterization of the autolytic enzymes of Clostridium perfringens.
|
| pubmed:publicationType |
Journal Article
|