Evidence that binding to the carboxyl-terminal heparin-binding domain (Hep II) dominates the interaction between plasma fibronectin and heparin
- 1 September 1988
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 27 (19) , 7565-7571
- https://doi.org/10.1021/bi00419a058
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 32 references indexed in Scilit:
- Characterization of fibronectin interactions with glycosaminoglycans and identification of active proteolytic fragments.Journal of Biological Chemistry, 1980
- Heparin enhances the rate of binding of fibronectin to collagenBiochemical Journal, 1980
- Structural basis for the anticoagulant activity of heparin. 1. Relationship to the number of charged groupsBiochemistry, 1979
- Isolation of a collagen-binding fragment from fibronectin and cold-insoluble globulin.Journal of Biological Chemistry, 1979
- The molecular-weight-dependence of the anti-coagulant activity of heparinBiochemical Journal, 1978
- Interactions among Heparin, Cold-Insoluble Globulin, and Fibrinogen in Formation of the Heparin-Precipitable Fraction of PlasmaJournal of Clinical Investigation, 1977
- Heterogeneity of the cold-insoluble globulin of human plasma (Clg), A circulating cell surface proteinBiochimica et Biophysica Acta (BBA) - Protein Structure, 1977
- Binding of soluble form of fibroblast surface protein, fibronectin, to collagenInternational Journal of Cancer, 1977
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976
- The separation of active and inactive forms of heparinBiochemical and Biophysical Research Communications, 1976