A route to 2',5'-oligoadenylates with increased stability towards phosphodiesterases.
The rates of enzymatic hydrolysis of 2',5'-oligoadenylates and their synthetic analogs have been measured. These compounds were treated with either NIH 3T3 cell lysates, mouse liver homogenates or snake venom phosphodiesterase. All analogs with 3'-terminal acyclic nucleoside residues demonstrated greater stability compared with the natural compound adenylyl(2'-5')adenylyl(2'-5')adenosine.
Itkes
A V
AV
Institute of Molecular Biology, USSR Academy of Sciences, Moscow.
Karpeisky MYa
Kartasheva
O N
ON
Mikhailov
S N
SN
Moiseyev
G P
GP
Pfleiderer
W
W
Charubala
R
R
Yakovlev
G I
GI
D000227:Adenine Nucleotides / Q000138:chemical synthesis / Q000378:metabolism; D000818:Animals; D002474:Cell-Free System; D066298:In Vitro Techniques; D051379:Mice; D009843:Oligoribonucleotides / Q000031:analogs & derivatives* / Q000138:chemical synthesis / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D013329:Structure-Activity Relationship
D000227:Adenine Nucleotides; D009843:Oligoribonucleotides; C023505:2',5'-oligoadenylate; D010727:Phosphoric Diester Hydrolases