Binding of heparin to human platelet factor 4
- 1 March 1986
- journal article
- research article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 234 (2) , 485-488
- https://doi.org/10.1042/bj2340485
Abstract
Platelet factor 4 is a small protein (Mr 7756) from the alpha-granules of blood platelets which binds strongly to and neutralizes the anticoagulant properties of heparin. From an analysis of X-ray crystallographic data a model for the binding of platelet factor 4 to heparin is proposed.This publication has 19 references indexed in Scilit:
- Solvent content of protein crystalsPublished by Elsevier ,2006
- X-ray diffraction analysis of crystals of bovine platelet factor 4Journal of Molecular Biology, 1984
- Dansyl (5-dimethylaminonaphthalene-1-sulphonyl)-heparin binds antithrombin III and platelet factor 4 at separate sitesBiochemical Journal, 1981
- Prediction of the secondary structure of platelet factor 4 and β-thromboglobulin from their amino acid sequencesThrombosis Research, 1981
- Evidence for a 3-O-sulfated D-glucosamine residue in the antithrombin-binding sequence of heparin.Proceedings of the National Academy of Sciences, 1980
- The molecular size of the antithrombin‐binding sequence in heparinFEBS Letters, 1980
- Platelet antiheparin proteins and antithrombin III interact with different binding sites on heparin moleculeFEBS Letters, 1979
- The molecular-weight-dependence of the anti-coagulant activity of heparinBiochemical Journal, 1978
- Studies on the Chemistry of Human Platelet Factor 4Pathophysiology of Haemostasis and Thrombosis, 1977
- Purification and binding properties of human platelet factor four.Journal of Biological Chemistry, 1976