动物脑组织中钙调蛋白的分离纯化

Separation And Purification Calmodulin in Animal Brain Tissue

本文主要以动物脑组织为材料,经热变性、离心、葡聚糖SephadexG-50分离纯化,通过紫外吸收图谱、二步酶解法检验钙调蛋白的纯度、浓度。结果显示,利用本法可分离纯化得到的钙调蛋白对PDE的激活倍数为83.3,比标准的钙调蛋白(对PDE的激活倍数为67.4)更具生物活性.

Animalm brain tissue was changed by denaturating, centifugating and sparating with Sephadex G-50 to purify. Then by means of UVS and two steps of enzymolysis to test the putiry and concentration. The result shows that the biological activity of the Calmodulin(to live multiple of arousing of PDE is 83.3), to compare with the standard Calmodulin, to more have the diological activity(to live multiple of PDE 67.4).