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Receptors for high molecular-weight kininogen on stimulated washed human-platelets

Academic Article
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Overview

authors

  • Greengard, J. S.
  • Griffin, John

publication date

  • 1984

journal

  • Biochemistry  Journal

abstract

  • Binding of human high molecular weight kininogen to washed human platelets was studied by measuring platelet-associated radiolabeled ligand in pellets of centrifuged platelets. High molecular weight kininogen was bound to stimulated platelets in the presence of ZnCl2 in a specific and saturable manner. Calcium ions potentiated ligand binding but did not substitute for zinc ions. Optimal binding of high molecular weight kininogen occurred near the plasma concentrations of both zinc and calcium ions. Scatchard analysis yielded 24 200 binding sites for high molecular weight kininogen with an apparent dissociation constant of 20 nM. These studies show that stimulated human platelets can bind many high molecular weight kininogen molecules with high affinity and suggest that the platelet surface may potentially serve as an important site for localizing the initial reactions of the plasma kinin-forming and intrinsic coagulation pathways.

subject areas

  • Adult
  • Blood Coagulation
  • Blood Platelets
  • Humans
  • In Vitro Techniques
  • Ions
  • Kinetics
  • Kininogens
  • Kinins
  • Molecular Weight
  • Receptors, Neurotransmitter
  • Receptors, Peptide
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Identity

International Standard Serial Number (ISSN)

  • 0006-2960

Digital Object Identifier (DOI)

  • 10.1021/bi00321a090

PubMed ID

  • 6099145
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Additional Document Info

start page

  • 6863

end page

  • 6869

volume

  • 23

issue

  • 26

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