Lambert R, Murthy M R
Neurochem Res. 1986 May;11(5):617-24. doi: 10.1007/BF00965331.
An RNase activity was found to be present in rat brain and liver and was strongly bound to the nucleoprotein fractions of these tissues. It could not be solubilized by treatment with acid or by lipid solvents. The pattern of oligonucleotides produced during hydrolysis by this enzyme indicated that it was probably an endonuclease with restricted specificity. It was inhibited by zinc ions and by low pH.
在大鼠脑和肝脏中发现了一种核糖核酸酶活性，并且它与这些组织的核蛋白部分紧密结合。用酸处理或脂质溶剂都不能使其溶解。该酶水解过程中产生的寡核苷酸模式表明，它可能是一种具有受限特异性的内切核酸酶。它受到锌离子和低pH值的抑制。
