[Hydrolysis and the products of 2',5'-oligoadenylate "core" cleavage]

"Core" 2',5'-oligoadenylates resistance to the action of phosphodiesterases was investigated by HPLC and the method of capillary electrophoresis. Oligoadenylate hydrolysis followed by the formation of adenosine and AMP was shown both in the case of incubation with the cells lysate and with the snake venoms phosphodiesterase. Kinetics of products formation in the process of enzymatic hydrolysis was analysed. In contrast to HPLC the method of capillary electrophoresis was observed to be more efficient for 2',5'-oligoadenylates hydrolysis products cleavage. The substance under study was shown not to have sufficient resistance to the enzyme and the latter, probably, hampers its therapeutic use.