Ebert C, Ebert G, Knipp H
Adv Exp Med Biol. 1977;86A:235-45. doi: 10.1007/978-1-4684-3282-4_14.
Hydroxyl groups in serine side chains of collagen, silk fibroin, and bovine serum albumin (BSA) were converted to SH by tosylation. In collagen film, 50% of the serine OH groups could be thiolated at most. In fibroin, only 13% because of its compact beta-pleated sheet structure and low susceptibility to swelling. The SH groups introduced are near enough together to form -S-S- bonds by oxidation. The residual SH content after oxidation was 0.1% in collagen and 0.03 to 0.25% in fibroin. Disulfide crosslinking increased the shrinkage temperature of collagen and fibroin and decreased the amount of shrinkage. BSA was crosslinked to dimers (MBSA) according to gel permeation chromatography and sedimentation analysis by the analytical centrifuge. Because these crosslinked proteins can be metabolized by the usual processes, in contrast to those crosslinked by artificial, nonphysiological bridges, they may be used for biological or medical purposes.
胶原蛋白、丝素蛋白和牛血清白蛋白（BSA）丝氨酸侧链中的羟基通过甲苯磺酰化转化为巯基。在胶原膜中，最多50%的丝氨酸羟基可被硫醇化。在丝素蛋白中，由于其紧密的β折叠片层结构和低溶胀敏感性，只有13%。引入的巯基彼此足够接近，可通过氧化形成-S-S-键。氧化后，胶原中的残余巯基含量为0.1%，丝素蛋白中的残余巯基含量为0.03%至0.25%。二硫键交联提高了胶原蛋白和丝素蛋白的收缩温度，并减少了收缩量。根据凝胶渗透色谱法和分析超速离心机的沉降分析，BSA交联形成了二聚体（MBSA）。与那些通过人工非生理性桥联交联的蛋白质不同，由于这些交联蛋白质可以通过常规过程进行代谢，因此它们可用于生物学或医学目的。
