SNase R与SNase酶学性质的比较研究

金黄色葡萄球菌核酸酶(SNase)的一种类似物SNase R在E.coli DH5x细胞中高效表达, 经磷酸纤维素离子交换柱层析纯化后.在SDS-PAGE上为一条分子量17.5KDa的蛋白带.本文对SNase R和SNase的某些酶学性质.酶动力学性质进行了比较研究.为蛋白质结构与功能及肽链折叠研究提供了又一种材料.

COMPARATIVE STUDIES ON THE ENZYMOLOGICAL CHARACTERISTICS OF SNase R AND SNase

SNase R, an analogue of staphylococcal nuclease (SNase) , which has additional six amino residues at its amino -terminus, was over-produced by recombinant DNA manipulation and purified by ion exchange chromatography on a phosphocellulose column. The purified enzyme gave a single band with a molecular weight of 17. 5KDa on SDS - polyacrylamide gel. The comparative studies of SNase R and SNase showed that the additional six amino acid residues at the N - terminus did not affect the Kinetic properties of the enzyme. The studies also provided an essential basis for using SNase R as a material for studying relationship between structure and function of protein, as well as polypeptide folding.