Magarill S A, Vasilenko S K, Raĭt V K
Biokhimiia. 1981 Mar;46(3):408-13.
An analysis of kinetic differences in homopolyribonucleotides hydrolysis by cobra venom endoribonuclease was carried out. It was concluded that the rate and intensity of hydrolysis as well as the length of the linear parts of the kinetic curves are correlated with the content of the nucleotide units with the C3'-endo conformation in the substrates. The structure factor was shown to predominate in some cases over the temperature factor. Protamine sulfate inhibits the enzyme by blocking its phosphodiether bonds. Study on the effects of divalent metal ions demonstrated the possibility that the enzyme-Me2+ complex is functionally active and that the ion-free polyribonucleotides are true substrates.
对眼镜蛇毒核糖核酸内切酶水解同聚核糖核苷酸的动力学差异进行了分析。得出的结论是，水解的速率和强度以及动力学曲线线性部分的长度与底物中具有C3'-内构象的核苷酸单元的含量相关。在某些情况下，结构因素比温度因素更占主导地位。硫酸鱼精蛋白通过阻断其磷酸二酯键来抑制该酶。对二价金属离子作用的研究表明，酶-Me2+复合物具有功能活性且无离子的聚核糖核苷酸是真正底物的可能性。
