Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1994-1-27
pubmed:abstractText
Prevotella loescheii PK1295 produces at least 3 proteases that are separable by isoelectric focusing. One of these proteases, an enzyme with an isoelectric point at 8.5 and an M(r) of 36,000, hydrolyzes the fimbria-associated adhesin on P. loescheii responsible for coaggregation with Streptococcus oralis 34, as well as gelatin, casein and fibrin. The action of this protease may contribute to the detachment of P. loescheii from its streptococcal coaggregation partner and provide a mechanism for bacterial relocation in dental plaque.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
D
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0902-0055
pubmed:author
pubmed:issnType
Print
pubmed:volume
8
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
283-7
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Adhesin degradation: a possible function for a Prevotella loescheii protease?
pubmed:affiliation
Laboratory of Microbial Ecology, National Institute of Dental Research, US National Institutes of Health, Bethesda, Maryland.
pubmed:publicationType
Journal Article