Schrader W P, Anderson J S
J Bacteriol. 1978 Feb;133(2):576-83. doi: 10.1128/jb.133.2.576-583.1978.
A membrane-bound nucleotidase of Bacillus cereus T was solubilized by digestion with trypsin and subsequently purified more than 300-fold. The purified nucleotidase was most active on ribonucleoside 5'-monophosphates and was slightly less active (40 to 60%) on deoxyribonucleoside 5'-monophosphates and ribonucleoside 3'-monophosphates. In addition to hydrolytic activity, the nucleotidase preparation possessed phosphotransferase activity by which phosphate is transferred from a phosphate donor to the 5' position of nucleosides.
蜡样芽孢杆菌T的一种膜结合核苷酸酶经胰蛋白酶消化后可溶解,随后纯化了300多倍。纯化后的核苷酸酶对5'-单磷酸核糖核苷活性最高,对5'-单磷酸脱氧核糖核苷和3'-单磷酸核糖核苷的活性略低(40%至60%)。除水解活性外,该核苷酸酶制剂还具有磷酸转移酶活性,可将磷酸从磷酸供体转移到核苷的5'位。