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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
1986-1-27
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pubmed:abstractText |
Factor XI is a dimeric protein and circulates in plasma complexed with high molecular weight kininogen (HMWK). We investigated the binding of HMWK to factor XIa utilizing two active site directed fluorescent probes: nitrobenzoxadiazole aminopentyl methylphosphonofluoridate for serine and dansyl-glu-gly-arg-chloromethyl ketone for histidine. In the presence of saturating amounts of HMWK, the fluorescence of factor XIa-fluorophore was quenched by approximately 28% for each probe. Titrations of the fluorescent factor XIa with HMWK revealed that each subunit of factor XIa binds one molecule of HMWK with a Kd approximately 3.4 X 10(-8)M.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-291X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
133
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
417-22
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:3936495-Binding Sites,
pubmed-meshheading:3936495-Factor XI,
pubmed-meshheading:3936495-Factor XIa,
pubmed-meshheading:3936495-Fluorescent Dyes,
pubmed-meshheading:3936495-Histidine,
pubmed-meshheading:3936495-Humans,
pubmed-meshheading:3936495-Kininogens,
pubmed-meshheading:3936495-Molecular Weight,
pubmed-meshheading:3936495-Protein Binding,
pubmed-meshheading:3936495-Serine,
pubmed-meshheading:3936495-Spectrometry, Fluorescence
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pubmed:year |
1985
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pubmed:articleTitle |
Stoichiometry of binding of high molecular weight kininogen to factor XI/XIa.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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