Hostname: page-component-586b7cd67f-t7czq Total loading time: 0 Render date: 2024-11-23T10:41:03.070Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of Biotinylation on Fibrinogen Function and Fibrinogen-Platelet Interaction

Published online by Cambridge University Press:  02 July 2020

JC Mattson ,
DW Estry ,
DM Farrah ,
HH Wolak  and
S Westley
JC Mattson
Affiliation:
>Department of Clinical Pathology, William Beaumont Hospital, Royal Oak, MI48073 and
DW Estry
Affiliation:
Medical Technology Program, Michigan State University, East Lansing, MI48824
DM Farrah
Affiliation:
>Department of Clinical Pathology, William Beaumont Hospital, Royal Oak, MI48073 and
HH Wolak
Affiliation:
>Department of Clinical Pathology, William Beaumont Hospital, Royal Oak, MI48073 and
Get access

Extract

Biotinylation of antibodies to be used in immunolocalization studies is a well established approach to mapping epitopes in biological specimens at both the light and ultrastructural level. Biotinylation of antibodies does not appear to significantly alter their interaction with antigen. A similar approach has been proposed for examining ligand interaction with receptors. Producing a soluble biotinylated ligand that behaves similarly to unlabeled ligand avoids the problems introduced by particulate labels such as ferritin, gold and latex. Particulate labels for ligands can be especially problematic in studies of receptor behavior in live cells since viable cells may directly react to the particulate probe itself. The interaction of plasma fibrinogen with its receptor on blood platelets, GPIIb-IIIa, is required for platelet-platelet cohesion and subsequent formation of a hemostatic platelet plug at sites of vascular injury. To study the events that follow binding of fibrinogen to its receptor5 we have produced a series of fibrinogens biotinylated with molar ratios of biotin:fibrinogen that range from 5 to 50.

Type
Cytochemistry, Histochemistry, Immunocytochemistry, and in Situ Hybridization
Information
Microscopy and Microanalysis , Volume 3 , Issue S2: Proceedings: Microscopy & Microanalysis '97, Microscopy Society of America 55th Annual Meeting, Microbeam Analysis Society 31st Annual Meeting, Histochemical Society 48th Annual Meeting, Cleveland, Ohio, August 10-14, 1997 , August 1997 , pp. 157 - 158
Copyright
Copyright © Microscopy Society of America 1997

Access options

Get access to the full version of this content by using one of the access options below. (Log in options will check for institutional or personal access. Content may require purchase if you do not have access.)

References

1. Guesdon, J.L.et al., J Histochem Cytochem 27(1979)1131.CrossRefGoogle Scholar

2. Hofmann, K.et al., Proc. Natl Acad Sci USA 74(1977)2697.CrossRefGoogle Scholar

3. Billingsley, M.L.et al., Proc. Natl Acad Sci USA 82(1985)7585.CrossRefGoogle Scholar

4. Peerschke, E.et al., Blood 55(1980)841.CrossRefGoogle Scholar

5. Hogan, M.et al., Ann NY Acad Sci 417(1994)282CrossRefGoogle Scholar