NDLI: High-affinity alpha-thrombin binding to platelet glycoprotein Ib alpha: identification of two binding domains.

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High-affinity alpha-thrombin binding to platelet glycoprotein Ib alpha: identification of two binding domains.

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High-affinity alpha-thrombin binding to platelet glycoprotein Ib alpha: identification of two binding domains.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Krutzsch, H. Fenton, J. W. Mckeown, L. P. Gralnick, H. R. Williams, S. Hansmann, K.
Description	Author Affiliation: Gralnick HR ( Hematology Service, National Institutes of Health, Bethesda, MD 20892.);
Abstract	alpha-Thrombin binding to and activation of platelets are of major importance in the initiation of physiologic thrombi and in the genesis of arterial thrombus formation. We have studied the site(s) and affinity of thrombin binding to human platelets. Our studies of the peptide inhibition of thrombin binding indicate that the glycoprotein Ib alpha binding site is of high affinity, Kd approximately 10(-10) M, while the seven-transmembrane-domain site is a moderate-affinity thrombin binding site, Kd approximately 10(-8) M. Further studies to modulate the high- or moderate-affinity thrombin binding can be directed to a specific class of sites. This would allow partial or total inhibition of specific thrombin-platelet interaction(s) in different clinical settings.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	14
Volume Number	91
Language	English
Publisher	National Academy of Sciences
Publisher Date	1994-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Blood Platelets Physiology Peptide Fragments Pharmacology Platelet Aggregation Drug Effects Platelet Membrane Glycoproteins Chemistry Metabolism Thrombin Amino Acid Sequence Binding Sites Kinetics Molecular Sequence Data Chemical Synthesis Peptide Mapping Peptides Structure-Activity Relationship Wasp Venoms Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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