摘要
:37℃下用胰蛋白酶水解SOD ,于 2 ,4,6 ,8和 1 0h对水解样及对照进行聚丙烯酰胺凝胶电泳 ,同时用邻苯三酚自氧化法测定酶活。结果表明 ,在体外SOD不能被胰蛋白酶水解 ,不同时间处理的SOD PAGE电泳谱带与对照完全一致。即活性染色均出现 4条带 ,蛋白染色均出现 6条带。 4条谱带于酶活性染色图谱中表明有酶活力 ,而另 2条无活力。胰蛋白酶水解处理后SOD活力呈明显下降趋势 ,水解 1 0h酶活降至原来的 80 %左右。与对照 37℃温度处理SOD活力下降趋势相同 ,推测可能是温度使酶变性对活力下降起主要作用。
SOD was degrated by trypsin at 37℃ Then the sample of SOD was conducted by means of PAGE after they were degrated for 2,4,6,8,10 hours At the same time,the assay pyrogallol autoxidation was used in determining SOD activity.The results showed that in vitro,SOD was resistant to trypsin's digestion.SOD PAGE pattern didn't vary with the length of degrated time It was similar to that of control Staining for protein of the PAGE pattern of SOD exhibits 6 bands:SOD 1,SOD 2,SOD 3,SOD 4,SOD 5 and SOD 6 There were 4 bands in activity stained pattern:SOD 1,SOD 2,SOD 3 and SOD 4 had activity of SOD However,SOD 5,SOD 6 had no activity The activity of degrated SOD obviously showed an decreasing tendency It remained 80% activity after SOD was degrated for 10 hours The temperature control had the same decreasing tendency It may be inferred that temperature had great influence on decreasing SOD activity by denaturating it
出处
《河北职业技术师范学院学报》
2000年第1期45-47,共3页
Journal of Hebei Vocation-Technical Teachers College
基金
河北职业技术师范学院青年科研基金
