麦芽根中の核酸分解酵素系とその応用に関する研究 : (第3報)リボ核酸分解条件の検討

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Influence of cations on the thermal stability of barley RNase was studied. RNase was stabilized in the presence of 10^<-3>M of Zn^<++>. The activities of RNase, 5'-nucleotidase and 3'-nucleotidase were inhibited by heavy metal ions, A barley extract degraded RNA to nucleoside 5'-monophosphates without a signigicant liberation of inorganic phosphate when it was treated in a thin RNA solution at a high temperature. The thermal stability of 5'-nucleotidase was affected by the concentrations of enzyme and sustrate, and it was difficult to obtain a high yield of nucleoside 5'-monophosphate with a high concentration of RNA.The yield of nucleoside 5'-monophosphate was more than 80% when the enzyme heated at 70℃ for 7.5 min in the preesnce of 10X^<-3>M of Zn^<++> was used.
公益社団法人日本生物工学会の論文
1968-08-25