Bowman E J, Altman S
Biochim Biophys Acta. 1980 Jun 13;613(2):439-47. doi: 10.1016/0005-2744(80)90098-4.
RNAase P (EC 3.1.26.5) activity has been identified in chick embryo thigh tissue on the basis of specific cleavage of Escherichia coli 129 nucleotide tRNATyr precursor and has been partially purified by the procedure used for human tissue culture KB cell RNAase P. RNAase P from chick resembles the KB cell RNAase P in substrate specificity, requirement for a divalent cation (Mg2+) and a monovalent cation (K+, Na+ or NH4+) for activity, inhibition by bulk tRNA, ready inactivation by proteases, and increasing instability; with purification. RNAase P activity is also present in whole chick embryos, as well as in liver and heart tissues. Furthermore, crude preparations of RNAase P from chick embryo heart tissue are relatively free of contaminating nucleases.
基于对大肠杆菌129个核苷酸的tRNATyr前体的特异性切割,已在鸡胚大腿组织中鉴定出核糖核酸酶P(EC 3.1.26.5)活性,并已通过用于人组织培养KB细胞核糖核酸酶P的方法进行了部分纯化。来自鸡的核糖核酸酶P在底物特异性、活性对二价阳离子(Mg2+)和一价阳离子(K+、Na+或NH4+)的需求、被大量tRNA抑制、易被蛋白酶灭活以及随着纯化而增加的不稳定性方面与KB细胞核糖核酸酶P相似。核糖核酸酶P活性也存在于整个鸡胚以及肝脏和心脏组织中。此外,来自鸡胚心脏组织的核糖核酸酶P粗制品相对不含污染性核酸酶。