施氏鲟免疫球蛋白酶解片段分析

Analysis of Immunoglobulin hydrolytic fragments of Amur sturgeon Acipenser schrenckii

采用几种蛋白水解酶对施氏鲟免疫球蛋白的酶解片段进行了分析。结果显示施氏鲟的免疫球蛋白在37℃条件下可以被木瓜蛋白酶、胃蛋白酶及胰蛋白酶分别裂解成不同的片段:木瓜蛋白酶的酶解片段出现在分子质量为130KDa、50KDa、10KDa和7KDa的蛋白谱带附近,而在酶量比较小、酶解时间较短的一组,在94KDa附近也有一条蛋白谱带;胃蛋白酶的水解片段,主要出现在分子质量为130KDa、94KDa、90KDa和32KDa的蛋白谱带附近;胰蛋白酶酶解片段主要为分子量为130KDa和74KDa的两条主带。

Immunoglobulin （Ig） fragments of Amur sturgeon Acipenser schrenckii hydrolyzed by several commonly used proteolytic enzymes were analyzed. The results show that Ig of Amur sturgeon can be hydrolyzed by trypsin, papain and pepsin into different fragments at 37℃. Bands with 130 KDa, 50 KDa, 10 KDa and 7 KDa protein were obtained after hydrolyzed by papain and a 94 KDa band was found at the beginning of hydrolyzing process while the amount of papain was less. The Ig fragments hydrolyzed by pepsin mainly appeared at bands of 130KDa, 94 KDa, 90 KDa and 32KDa. Main Ig fragments hydrolyzed by trypsin can be detected at 130 KDa and 74 KDa. While the amount of enzyme and hydrolytic time increasing, some bands disappeared and that of larger molecular weight disappeared early.