Weller D L, Richman A, Specht C
Mol Biochem Parasitol. 1981 Nov;4(1-2):1-7. doi: 10.1016/0166-6851(81)90023-2.
Two bands of RNAase activity were observed on gel electrophoresis of fractions obtained during partial purification of the RNAase of Entamoeba invadens. The faster migrating band which was responsible for most of the RNAase activity was isolated by gel electrophoresis. A pI of 5.5 was determined for this RNAase activity and estimates of its molecular weight and sedimentation coefficient gave values of about 25 000 and approximately 2.8 S. It exhibited maximum activity around pH 6, and digestion of RNA showed a pattern expected of an endoribonuclease.
在对侵袭内阿米巴核糖核酸酶进行部分纯化过程中获得的各组分进行凝胶电泳时,观察到两条核糖核酸酶活性带。通过凝胶电泳分离出了迁移速度较快的带,该带具有大部分核糖核酸酶活性。测定该核糖核酸酶活性的等电点为5.5,其分子量和沉降系数的估计值分别约为25000和2.8S。它在pH6左右表现出最大活性,对RNA的消化呈现出内切核糖核酸酶预期的模式。