Salikhova Z Z, Sokolova R B, Ponomareva A Z, Iusupova D V
Kazan State University, Kazan, 420008 Russia.
Prikl Biokhim Mikrobiol. 2001 Jan-Feb;37(1):43-7.
Two isoforms of nuclease displaying DNase and RNase activities were found in the culture liquid and periplasm of Proteus mirabilis. The enzyme was isolated from the periplasm and then purified to a functionally homogeneous state. The nuclease was equally potent in cleaving denatured and native DNAs by the endonuclease mechanism and was designated Pm endonuclease. The endonuclease was shown to be a temperature-dependent enzyme with a pH optimum of 10.4-10.6, requiring the presence of bivalent metal ions and inhibited by citrate and ethylenediaminetetraacetate.
在奇异变形杆菌的培养液和周质中发现了两种具有脱氧核糖核酸酶（DNase）和核糖核酸酶（RNase）活性的核酸酶同工型。该酶从周质中分离出来，然后纯化至功能均一的状态。这种核酸酶通过核酸内切酶机制切割变性DNA和天然DNA的能力相当，被命名为奇异变形杆菌核酸内切酶（Pm endonuclease）。该核酸内切酶是一种温度依赖性酶，最适pH为10.4 - 10.6，需要二价金属离子存在，且受柠檬酸盐和乙二胺四乙酸抑制。
