Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Science 24 April 1981:
Vol. 212. no. 4493, pp. 457 - 459
DOI: 10.1126/science.7209542

Articles

Science, Vol 212, Issue 4493, 457-459
Copyright © 1981 by American Association for the Advancement of Science


articles

Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen

AP Laudano and RF Doolittle

The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. In contrast, there is no significant increase in the affinity of peptides beginning with the amino terminal sequence of the fibrin alpha chain, Gly-Pro-Arg, in the presence of calcium ions, although the number of binding sites increases. In the latter case, the increased number of sites is due to the alpha chain analogs binding to the site ordinarily occupied by the beta chain analogs. These results indicate that structures at the amino terminus of the fibrin beta chain play a more important role in fibrin polymerization when calcium ions are present.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The fibrin-derived {gamma}377-395 peptide inhibits microglia activation and suppresses relapsing paralysis in central nervous system autoimmune disease.
R. A. Adams, J. Bauer, M. J. Flick, S. L. Sikorski, T. Nuriel, H. Lassmann, J. L. Degen, and K. Akassoglou (2007)
J. Exp. Med. 204, 571-582
   Abstract »    Full Text »    PDF »
Polymerization of fibrin: direct observation and quantification of individual B:b knob-hole interactions.
R. I. Litvinov, O. V. Gorkun, D. K. Galanakis, S. Yakovlev, L. Medved, H. Shuman, and J. W. Weisel (2007)
Blood 109, 130-138
   Abstract »    Full Text »    PDF »
gamma -Chain Dysfibrinogenemias: Molecular Structure-Function Relationships of Naturally Occurring Mutations in the gamma  Chain of Human Fibrinogen.
H. C.F. Cote, S. T. Lord, and K. P. Pratt (1998)
Blood 92, 2195-2212
   Full Text »    PDF »
Antibodies Against the Fibrin ß-Chain Amino-Terminus Detect Active Canine Venous Thrombi.
T. A. Morris, J. J. Marsh, R. Konopka, C. A. Pedersen, P. G. Chiles, R. Fagnani, M. Hagan, and K. M. Moser (1997)
Circulation 96, 3173-3179
   Abstract »    Full Text »
The Polymerization Pocket "a" within the Carboxyl-terminal Region of the gamma  Chain of Human Fibrinogen Is Adjacent to but Independent from the Calcium-binding Site.
H. C. F. Cote, K. P. Pratt, E. W. Davie, and D. W. Chung (1997)
J. Biol. Chem. 272, 23792-23798
   Abstract »    Full Text »    PDF »



To Advertise     Find Products


Science. ISSN 0036-8075 (print), 1095-9203 (online)