Key result
An enzyme tentatively designated Y-pUpN PDE specifically splits the covalent bond between VPg and picornaviral RNAs, but does not unlink VPg from comoviral RNA.
Identification and partial purification of a novel enzyme (Y-pUpN PDE) that specifically cleaves the bond between VPg and picornaviral RNAs.
Y-pUpN PDE selectively processes picornaviral RNAs; leaves open its physiological role and antiviral applications.
An enzyme which specifically splits a covalent bond between VPg and picornaviral RNAs (tentatively designated Y-pUpN PDE) has been partially purified from mouse ascites Krebs II cells. Using substrates labelled in vitro with 125I-Bolton-Hunter reagent and a new assay based on Kieselgel thin-layer chromatography, several biochemical characteristics of the enzyme have been determined, depending on the pH and on Mg2+, K+, spermidine and PEG concentrations, etc. We found that the enzyme does not 'unlink' VPg from comoviral RNA. We suggest that Y-pUpN PDE represents a new class of enzymes.
No takes yet. Share an insight, caveat, or question.
Drygin et al. (1988) studied this question. Y-pUpN PDE enzyme was evaluated on Enzyme characteristics and activity on VPg-picornaviral RNA bond. An enzyme tentatively designated Y-pUpN PDE specifically splits the covalent bond between VPg and picornaviral RNAs, but does not unlink VPg from comoviral RNA.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: