[An enzyme hydrolyzing the covalent bond between RNA and VPg of picornaviruses. Substrates and methods of analysis of activity].
Some new substrates--RNA-VPg, RNA-peptide and a small fragment of RNA peptide--labelled at the peptide component with [125I]Bolton-Hunter reagent have been proposed for use in the isolation and characterization of the enzyme hydrolyzing the phosphodiester bond between the VPg protein and encephalomyocarditis virus RNA. A novel procedure for the analysis of the specific enzyme activity is based on thin-layer chromatography of hydrolytic products on silicagel or polyethylenimine cellulose. The molecular mass of the enzyme isolated by a modified procedure involving FPLC is 90-95 kD.
Drygin
Iu F
IuF
Shabanov
A A
AA
Bogdanov
A A
AA
D000818:Animals; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004686:Encephalomyocarditis virus / Q000378:metabolism*; D006868:Hydrolysis; D007202:Indicators and Reagents; D051379:Mice; D008970:Molecular Weight; D010446:Peptide Fragments / Q000378:metabolism; D010727:Phosphoric Diester Hydrolases / Q000302:isolation & purification / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D013379:Substrate Specificity; D013388:Succinimides; D014758:Viral Core Proteins / Q000378:metabolism*
D007202:Indicators and Reagents; D010446:Peptide Fragments; D012367:RNA, Viral; D013388:Succinimides; D014758:Viral Core Proteins; C022581:Bolton-Hunter reagent; D010727:Phosphoric Diester Hydrolases
Ferment, gidroliziruiushchiĭ kovalentnuiu sviaz' mezhdu RNK i VPg pikornavirusov. Substraty i metody analiza aktivnosti.