Evidence of random structural features in the heparin polymer.
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.
D000818:Animals; D000990:Antithrombin III; D001665:Binding Sites; D003201:Computers; D006493:Heparin / Q000302:isolation & purification; D019763:Heparin Lyase; D008968:Molecular Conformation; D011108:Polymers; D011133:Polysaccharide-Lyases; D013552:Swine
D011108:Polymers; D000990:Antithrombin III; D006493:Heparin; D011133:Polysaccharide-Lyases; D019763:Heparin Lyase