John R, Tyagi R, Gupta M N
Chemistry Department, IIT Delhi, India.
Biochem Mol Biol Int. 1994 May;33(2):263-72.
Chemical aggregation of bovine serum albumin by extensive chemical crosslinking with glutaraldehyde yielded an insoluble protein preparation with significant antiproteolytic activity. This was presumably due to the presence of alpha 2-macroglobulin in bovine serum albumin preparations. Chemical crosslinking of bovine serum albumin under optimum conditions was found to increase its antitryptic activity by about four times. The results indicate that enhanced rigidity of alpha 2-macroglobulin structure increases its antitryptic activity.
通过与戊二醛进行广泛化学交联使牛血清白蛋白发生化学聚集，得到了一种具有显著抗蛋白水解活性的不溶性蛋白质制剂。这可能是由于牛血清白蛋白制剂中存在α2-巨球蛋白。发现在最佳条件下对牛血清白蛋白进行化学交联可使其抗胰蛋白酶活性提高约四倍。结果表明，α2-巨球蛋白结构刚性的增强会提高其抗胰蛋白酶活性。
