Ye X Y, Ng T B
Department of Biochemistry, The Chinese University of Hong Kong, Shatin, New Territories, Hong Kong, China.
J Pept Sci. 2003 Feb;9(2):120-4. doi: 10.1002/psc.437.
A ribonuclease (RNase), possessing an N-terminal sequence disparate from those of ribonucleases from other mushrooms and previously isolated Pleuotus ostreatus RNases, was purified from the fruiting bodies of the edible mushroom Pleurotus ostreatus. The N-terminal sequence of Pleurotus ostreatus RNase did not manifest homology even to a previously reported RNase from the same mushroom. The ribonuclease was adsorbed on CM-Sepharose and Mono S. It exhibited a molecular mass of 12 kDa in both sodium dodecyl sulphate-polyacrylamide gel electrophoresis and gel filtration on Superdex 75. The ribonuclease displayed an activity of 11490 U/mg on yeast tRNA. The highest ribonuclease activity was exhibited toward poly U, followed by poly A and poly C. No activity was shown toward poly G. The optimal pH for its activity was 7 and the optimal temperature was 55 degrees C. It inhibited cell-free translation in a rabbit reticulocyte lysate with an IC50 of 240 nM.
从食用菌平菇的子实体中纯化出一种核糖核酸酶（RNase），其N端序列与其他蘑菇的核糖核酸酶以及先前分离的平菇核糖核酸酶不同。平菇核糖核酸酶的N端序列甚至与之前报道的来自同一蘑菇的核糖核酸酶也没有同源性。该核糖核酸酶可吸附于CM - 琼脂糖凝胶和Mono S上。在十二烷基硫酸钠 - 聚丙烯酰胺凝胶电泳和Superdex 75凝胶过滤中，它均显示分子量为12 kDa。该核糖核酸酶对酵母tRNA的活性为11490 U/mg。其对多聚U的核糖核酸酶活性最高，其次是多聚A和多聚C，对多聚G无活性。其活性的最适pH为7，最适温度为55℃。它在兔网织红细胞裂解物中抑制无细胞翻译，IC50为240 nM。
