Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1981-9-15
pubmed:abstractText
Binding of fibrinogen degradation products was measured to Gram-positive cocci known to carry receptors for human fibrinogen. Forty-one strains of S. aureus and group A, C and G streptococci were studied. The largest plasmin produced fragment (X-fragment, HMWDP) showed higher binding levels to the bacterial receptors in all four species as compared to intact fibrinogens. The enzymatically produced C-terminal fragment D was strongly reactive, whereas the N-terminal fragment E was non-reactive. Inhibition experiments showed that reactive fragments were bound to the same receptors as fibrinogen. Three chemically-produced and well-characterized fragments from the terminal and the middle portions of the fibrinogen molecule were all negative in binding assays. The binding patterns for fibrinogen and the fragments tested were identical in the four bacterial species tested, S. aureus and group A, C and G streptococci. The results confirm and extend earlier data on similarities between fibrinogen receptors on these Gram-positive bacterial species.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0105-0656
pubmed:author
pubmed:issnType
Print
pubmed:volume
89
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
49-55
pubmed:dateRevised
2009-6-4
pubmed:meshHeading
pubmed:year
1981
pubmed:articleTitle
Binding of fibrinogen degradation products to S. aureus and to beta-hemolytic streptococci group A, C and G.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't