Linked Life Data

2977421

Source:http://linkedlifedata.com/resource/pubmed/id/2977421

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1989-6-8
pubmed:abstractText
Certain Group A beta-hemolytic streptococci express a receptor that is capable of specifically binding the human plasma protease plasmin. Once bound, plasmin remains enzymatically active and is unregulated by its naturally occurring inhibitor alpha-2-antiplasmin (Lottenberg, R., C. C. Broder and M. D. P. Boyle, 1987. Infect. Immun. 55: 1914-1918). In this study certain characteristics of the interaction between plasmin and the receptor expressed on a group A beta-hemolytic streptococcus, strain 64/14, were examined. Binding occurred optimally at physiologic pH and ionic strength. The KD was 5 x 10(-11) M and there were approximately 800 receptors per bacterium. Mouse passage of strain 64 had no significant effect on the KD of the receptor. Binding of plasmin to the bacteria was inhibited by lysine and epsilon-aminocaproic acid in a concentration dependent manner. Similarly these amino acids would displace pre-bound plasmin from the bacteria. These findings suggest a role for plasmin's high affinity lysine binding site in the interaction of plasmin with the bacteria.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0882-4010
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
19-27
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1988
pubmed:articleTitle
Characterization of the interaction of human plasmin with its specific receptor on a group A streptococcus.
pubmed:affiliation
Department of Medicine, College of Medicine, University of Florida, Gainesville 32610.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, Non-U.S. Gov't