[An enzyme hydrolyzing the covalent bond between RNA and VPg of picornaviruses. Substrates and methods of analysis of activity]. / Ferment, gidroliziruiushchii kovalentnuiu sviaz' mezhdu RNK i VPg pikornavirusov. Substraty i metody analiza aktivnosti.
Biokhimiia
; 53(8): 1371-9, 1988 Aug.
Article
en Ru
| MEDLINE
| ID: mdl-2847820
ABSTRACT
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.
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Banco de datos:
MEDLINE
Asunto principal:
ARN Viral
/
Proteínas del Núcleo Viral
/
Hidrolasas Diéster Fosfóricas
/
Virus de la Encefalomiocarditis
Límite:
Animals
Idioma:
Ru
Año:
1988
Tipo del documento:
Article