The molecular size of the antithrombin‐binding sequence in heparin
- 11 August 1980
- journal article
- Published by Wiley in FEBS Letters
- Vol. 117 (1-2), 203-206
- https://doi.org/10.1016/0014-5793(80)80945-8
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Structure of the antithrombin-binding site in heparin.Proceedings of the National Academy of Sciences, 1979
- Identification of N-sulphated disaccharide units in heparin-like polysaccharidesBiochemical Journal, 1979
- Correlation between structure and function of heparinProceedings of the National Academy of Sciences of the United States of America, 1979
- Periodate oxidation of the d-glucuronic acid residues in heparan sulphate and heparinCarbohydrate Research, 1978
- Anticoagulant properties of heparin fractionated by affinity chromatography on matrix-bound antithrombin III and by gel filtrationThrombosis Research, 1976
- Anticoagulant activity of heparin: Isolation of antithrombin‐binding sitesFEBS Letters, 1976
- Anticoagulant activity of heparin: Separation of high‐activity and low‐activity heparin species by affinity chromatography on immobilized antithrombinFEBS Letters, 1976
- Biosynthesis of heparin. Loss of C-5 hydrogen during conversion of d-glucuronic to l-iduronic acid residuesBiochemical and Biophysical Research Communications, 1976
- The separation of active and inactive forms of heparinBiochemical and Biophysical Research Communications, 1976
- The distribution of 2-acetamido-2-deoxy-D-glucose residues in mammalian heparinsCarbohydrate Research, 1972