Collect. Czech. Chem. Commun. 1981, 46, 1059-1067

Ribonuclease activiy associated with chick embryo chorioallantoic plasma membranes

Svetlana Pristašová and Marta Rosenbergová

Institute of Virology, Slovak Academy of Sciences, 809 39 Bratislava


Ribonuclease activiy was found associated with plasma membranes isolated from chick embryo chorioallantoic cells. The enzyme was solubilized with buffered 1% Triton X-100 and purified 40-fold by 1-butanol extraction and gel-filtration on Sephadex G-100. The purified Rnase was found to be free of deoxyribonuclease, alkaline phosphatase and decyclizing 2',3'-phosphodiesterase activities. the enzyme is capable to degrade RNA and polycytidylic acid into acid-soluble oligonucleotides terminated in 3'-phosphate. No nucleoside monophosphates and 2',3'-cyclic nucleoside monophosphates were detected. The optimal pH of RNA and poly C hydrolysis were 7.2 and 7.8, the optimal temperatures 60 and 45°C, respectively. The purified enzyme is thermolabile, and it requires monovalent cations for the full enzyme activity.