Parsons M, Romeo G
Clin Chim Acta. 1980 Jan 31;100(3):215-24. doi: 10.1016/0009-8981(80)90269-7.
alpha 2-Macroglobulin was purified from plasma of five cystic fibrosis patients and five normal controls. SDS gel electrophoresis of native alpha 2-macroglobulin from cystic fibrosis patients and normal donors showed identical subunit molecular weights, as did trypsin cleavage products. Cystic fibrosis and control alpha 2-macroglobulins were indistinguishable by isoelectric focusing and exhibited appropriate shifts in isoelectric point following binding of trypsin. The trypsin-binding capacities of control and cystic fibrosis alpha 2-macroglobulins did not differ, nor did the esterolytic activity of the trypsin-alpha 2-macroglobulin complexes.
从五名囊性纤维化患者和五名正常对照者的血浆中纯化出α2-巨球蛋白。囊性纤维化患者和正常供体的天然α2-巨球蛋白的SDS凝胶电泳显示亚基分子量相同，胰蛋白酶裂解产物也是如此。通过等电聚焦无法区分囊性纤维化和对照α2-巨球蛋白，并且在胰蛋白酶结合后等电点出现了适当的偏移。对照和囊性纤维化α2-巨球蛋白的胰蛋白酶结合能力没有差异，胰蛋白酶-α2-巨球蛋白复合物的酯酶活性也没有差异。
