Silver F H, Yannas I V, Salzman E W
J Biomed Mater Res. 1979 Sep;13(5):701-16. doi: 10.1002/jbm.820130504.
Precipitation of bovine hide collagen by chondroitin 6-sulfate at low pH and subsequent crosslinking enhances the blood compatibility of native collagen. Both dehydrothermal crosslinking and complexation with chrondroitin 6-sulfate separately decrease the platelet-aggregating activity of collagen. Crosslinking also decreases the number of free acidic and free basic residues on collagen, which suggests that crosslinking involves these residues in condensation reactions with formation of intrachain and interchain synthetic peptide bonds. Clotting times for collagen precipitated with chondroitin 6-sulfate indicate that this surface does not activate or interfere with coagulation via either the intrinsic or extrinsic pathway. These findings support further consideration of collagen modified by chondroitin 6-sulfate as a blood compatible material.
在低pH值下，硫酸软骨素6沉淀牛皮胶原蛋白，随后进行交联，可增强天然胶原蛋白的血液相容性。脱氢热交联和与硫酸软骨素6络合分别降低了胶原蛋白的血小板聚集活性。交联还减少了胶原蛋白上游离酸性和游离碱性残基的数量，这表明交联涉及这些残基在缩合反应中形成链内和链间合成肽键。硫酸软骨素6沉淀的胶原蛋白的凝血时间表明，该表面不会通过内源性或外源性途径激活或干扰凝血。这些发现支持进一步考虑将硫酸软骨素6修饰的胶原蛋白作为血液相容性材料。
