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Fluorescein derivatization of fibrinogen for flow cytometric analysis of fibrinogen binding to platelets

✍ Scribed by Eric Heilmann; Laurie A. Hynes; Samuel A. Burstein; James N. George; George L. Dale

Publisher
John Wiley and Sons
Year
1994
Tongue
English
Weight
678 KB
Volume
17
Category
Article
ISSN
0196-4763

No coin nor oath required. For personal study only.

✦ Synopsis

Dog and human fibrinogen were derivatized with N-hydroxysuccinimidofluorescein and utilized for flow cytometric estimation of fibrinogen binding to activated platelets. Fluorescein-fibrinogen binding fulfilled the criteria for specific binding to platelets; the binding was saturable, dependent on agonist activation, and inhibited by unlabeled fibrinogen. In addition, EDTA and barbourin, a KGD-containing peptide, were found to inhibit the binding of fluorescein-fibrinogen. Fluorescein-fibrinogen bound to dog platelets with an apparent affinity of 0.31 p M after stimulation with either adenosine-5'-diphosphate (ADP) or plateletac-tivating factor. The labeled fibrinogen was also used to study the fibrinogen binding capacity of aged, biotinylated platelets. Aged platelets were indistinguishable from young platelets with re- gard to fibrinogen binding in response to ADP. These studies document that direct derivatization of fibrinogen with fluorescein generates a useful probe for analyzing fibrinogen binding to platelets with flow CytOmetry.

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