[Characteristics of an enzyme hydrolyzing the covalent bond between RNA and protein VPg of the encephalomyocarditis virus].
The enzyme termed by us as uridilylpolynucleotide-(5'P----O)-tyrosine phosphodiesterase (Y-pUpN PDE) was isolated from mouse ascites Krebs II cells by ion-exchange and affinity chromatography. The enzyme was found to specifically split the natural covalent bond between VPg and EMC or polio viral RNAs. The enzyme is completely inactivated at 55 degrees C and partially by EDTA. The enzyme preparation isolated by the above-mentioned procedure is not homogeneous and contains inhibiting admixture(s). Possible role of the enzyme in living cells is discussed.
D000595:Amino Acid Sequence; D000818:Animals; D002287:Carcinoma, Krebs 2 / Q000201:enzymology*; D002846:Chromatography, Affinity; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004686:Encephalomyocarditis virus / Q000378:metabolism*; D006367:HeLa Cells / Q000201:enzymology; D006801:Humans; D006868:Hydrolysis; D051379:Mice; D010727:Phosphoric Diester Hydrolases / Q000378:metabolism*; D012367:RNA, Viral / Q000378:metabolism*; D014758:Viral Core Proteins; D014764:Viral Proteins / Q000378:metabolism*
D012367:RNA, Viral; D014758:Viral Core Proteins; D014764:Viral Proteins; D010727:Phosphoric Diester Hydrolases; C025672:RNA-tyrosine phosphatase
Kharakteristika fermenta, gidrolizuiushchego prirodnuiu kovalentnuiu sviaz' mezhdu RNK i belkom VPg virusa entsefalomiokardita.