Abstract
Partial purification of the encephalomyocarditis protease synthesized in extracts from rabbit reticulocytes shows that the activity responsible for cleaving coat precursor protein cosediments with a previously unmapped virus-coded protein with an apparent molecular weight of 20,000. Tryptic analysis shows that this protein is derived from protein D, a virus-coded component of the encephalomyocarditis RNA polymerase.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Capsid / metabolism
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Centrifugation, Density Gradient
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DNA-Directed RNA Polymerases / analysis*
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DNA-Directed RNA Polymerases / genetics
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Encephalomyocarditis virus / analysis
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Encephalomyocarditis virus / enzymology*
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Encephalomyocarditis virus / genetics
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Genes, Viral
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Peptide Hydrolases / isolation & purification*
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Peptide Hydrolases / metabolism
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Protein Precursors / metabolism
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Viral Proteins / analysis
Substances
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Protein Precursors
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Viral Proteins
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DNA-Directed RNA Polymerases
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Peptide Hydrolases