Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1994-3-1
pubmed:abstractText
The localization of regions of fibrinogen that inhibit coaggregation between Porphyromonas gingivalis and Streptococcus oralis was investigated. The coaggregation was inhibited by A alpha and gamma chains, but not by B beta chain. The inhibitory activity of fragment D was more potent than that of fragment E. Some cyanogen bromide-treated fragments isolated from A alpha and gamma chains including the NH2-terminal 148-207 amino acid residues of A alpha chain (A alpha 148-207) and gamma 1-78 showed inhibitory activities. A alpha 148-207 was further digested with lysyl endopeptidase. A alpha 158-176 and A alpha 192-206 which contained four and two arginine residues, respectively, retained the inhibitory activities. When the arginine residues of these two peptides were modified by phenylglyoxal, the inhibitory activities were much reduced. These findings suggest that the arginine residues of some specific regions of fibrinogen may play an important role in the inhibition of the coaggregation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
114
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
31-6
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Inhibition of coaggregation between Porphyromonas gingivalis and Streptococcus oralis by fibrinogen fragments.
pubmed:affiliation
Department of Preventive Dentistry, Faculty of Dentistry, Osaka University, Japan.
pubmed:publicationType
Journal Article