Evidence of random structural features in the heparin polymer
- 17 December 1985
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 24 (26), 7805-7810
- https://doi.org/10.1021/bi00347a045
Abstract
The first use of computer-simulation studies to examine heparin''s structure has been reported. The product distributions obtained when porcine mucosal heparins were depolymerized with heparinase have been compared to computer-simulated distributions. The modeled distribution was relatively unaffected by the polydispersity and molecular weight of heparin. However, the percent of heparinase-cleavable glycosidic linkages and their distribution throughout the polymer resulted in a marked change in the simulated product distribution. The similarity between experimentally observed and computer-simulated product distributions is consistent with the random distribution of heparinase-cleavable sites in porcine mucosal heparin. Finally, a random distribution of N-acetyl residues with respect to heparinase-cleavable sites was experimentally observed.This publication has 18 references indexed in Scilit:
- Differential anticoagulant activity of heparin fragments prepared using microbial heparinase.Journal of Biological Chemistry, 1982
- Mode of action of heparin lyase on heparinBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982
- Multiple functional domains of the heparin molecule.Proceedings of the National Academy of Sciences, 1981
- Purification of heparinase and heparitinase by affinity chromatography on glycosaminoglycan-bound ah-sepha-rose 4bCarbohydrate Research, 1981
- Heparinase production by Flavobacterium heparinumApplied and Environmental Microbiology, 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
- Structure of the antithrombin-binding site in heparin.Proceedings of the National Academy of Sciences, 1979
- Purification of chondroitinase B and chondroitinase C using glycosaminoglycan-bound AH-Sepharose 4BCarbohydrate Research, 1979
- The molecular-weight-dependence of the anti-coagulant activity of heparinBiochemical Journal, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976