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J Virol. 1974 August; 14(2): 282-291
Copyright © 1974 American Society for Microbiology. All Rights Reserved.

Characterization of the Large Picornaviral Polypeptides Produced in the Presence of Zinc Ion

Byron E. Butterworth and Bruce D. Korant

1 Central Research Department, E. I. du Pont de Nemours and Company, Wilmington, Delaware 19898

ABSTRACT

Zinc ion inhibits the posttranslational cleavages of human rhinovirus-1A, encephalomyocarditis virus, and poliovirus polypeptides. Each virus displayed a different susceptibility to zinc. However, in each case the cleavages of the capsid precursor and the cleavages analogous to the C -> D -> E conversion in encephalomyocarditis virus were most sensitive to zinc. Higher concentrations of zinc resulted in the buildup of even larger precursor polypeptides of a size between 106,000 and 214,000 daltons. The sizes of these polypeptides and the relative position of their gene loci on the viral RNA were determined. These data were used to place these polypeptides in the over-all scheme of viral protein processing.


J Virol. 1974 August; 14(2): 282-291
Copyright © 1974 American Society for Microbiology. All Rights Reserved.




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Copyright © 1974 by the American Society for Microbiology. All rights reserved.