Krupianko V I, Bezborodova S I
Biokhimiia. 1976 Aug;41(8):1442-7.
In studies of splitting of transferase substrates cytidylyl-(3' leeds to 5')-adenosine and adenylyl-(3'leds to to 5')-cytidine by Penicillium brevicompactum RNAase the pH-optimum activity of enzyme has been found to fall within the range of 4.7 +/- 0;1; temperature optimum--within 41 degrees--43 degrees C; adenine-nucleotides, their constituent components and polyphosphates display the properties of competitive inhibitors on splitting substrates and that amino-acid residues (presumably weakly- and strongly-protonated imidasole groups) function in the active site of this enzyme (pK 5.88 +/- 0,1 AND 6.6 +/- 0.1). A comparison of some physico-chemical and kinetic parameters of Penicillium breviocompactum RNAse to those of other nonspecific RNAses of fungi is made.
在短密青霉核糖核酸酶对转移酶底物胞苷酰 -（3' 至 5'）-腺苷和腺苷酰 -（3' 至 5'）-胞苷的裂解研究中，已发现该酶的最适pH活性在4.7±0.1范围内；最适温度在41℃至43℃之间；腺嘌呤核苷酸、其组成成分和多磷酸盐对底物裂解表现出竞争性抑制剂的特性，并且氨基酸残基（可能是弱质子化和强质子化的咪唑基团）在该酶的活性位点起作用（pK为5.88±0.1和6.6±0.1）。对短密青霉核糖核酸酶与真菌其他非特异性核糖核酸酶的一些物理化学和动力学参数进行了比较。
