Structure and affinity for antithrombin of heparan sulfate chains derived from basement membrane proteoglycans.
Open Access
- 1 April 1987
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 262 (11) , 5036-5043
- https://doi.org/10.1016/s0021-9258(18)61150-0
Abstract
No abstract availableThis publication has 30 references indexed in Scilit:
- Anticoagulantly active heparin from clam (Mercenaria mercenaria)Archives of Biochemistry and Biophysics, 1986
- Isolation and characterization of a heparin with high anticoagulant activity from Anomalocardia brasilianaBiochimica et Biophysica Acta (BBA) - General Subjects, 1985
- Contribution of monosaccharide residues in heparin binding to antithrombin IIIBiochemistry, 1985
- Heparinlike molecules with anticoagulant activity are synthesized by cultured endothelial cellsBiochemical and Biophysical Research Communications, 1985
- Structure and interactions of heparan sulfate proteoglycans from a mouse tumor basement membraneEuropean Journal of Biochemistry, 1984
- Further characterization of the antithrombin-binding sequence in heparinCarbohydrate Research, 1982
- Glycosaminoglycans and Their Binding to Biological MacromoleculesAnnual Review of Biochemistry, 1978
- Formation of anhydrosugars in the chemical depolymerization of heparinBiochemistry, 1976
- Anticoagulant activity of heparin: Separation of high‐activity and low‐activity heparin species by affinity chromatography on immobilized antithrombinFEBS Letters, 1976
- Changes in the fine structure of the parietal yolk sac of the rat placenta with increasing gestational ageJournal of Anatomy, 1968