title: [Hydrolytic stability of a covalent AMP-RNA ligase complex].
abstract: Behavior of the covalent [32P]- and [14C]AMP-RNA ligase complex under various conditions has been studied. The covalent structure is shown to be readily cleaved by acid and hydroxylamine and relatively stable to alkali and snake venom phosphodiesterase. Products of degradation of the AMP-RNA ligase and AMP-DNA ligase complexes were compared. The data obtained support the earlier assumption of a phosphoamide bond in the AMP-RNA ligase compound.
mesh_terms: D000249:Adenosine Monophosphate / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002854:Chromatography, Paper; D004591:Electrophoresis, Polyacrylamide Gel; D006868:Hydrolysis; D006898:Hydroxylamines / Q000494:pharmacology; D066298:In Vitro Techniques; D010727:Phosphoric Diester Hydrolases / Q000494:pharmacology; D011118:Polynucleotide Ligases / Q000378:metabolism*; D011130:RNA Ligase (ATP) / Q000378:metabolism*; D012910:Snake Venoms / Q000494:pharmacology
chemical_list: D006898:Hydroxylamines; D012910:Snake Venoms; D000249:Adenosine Monophosphate; D010727:Phosphoric Diester Hydrolases; D011118:Polynucleotide Ligases; D011130:RNA Ligase (ATP)
vernacular_title: Gidroliticheskaia ustoĭchivist' kovalentnogo AMP-RNK-ligaznogo kompleksa.