Virus-Specific Proteins Synthesized in Encephalomyocarditis Virus-Infected HeLa Cells

摘要: Abstract The in vivo synthesis of encephalomyocarditis-specific proteins was studied by labeling the viral with radioactive amino acids under conditions where host-protein almost completely inhibited. To assure recovery all proteins, intact cells were lysed hot 1% sodium dodecyl sulfate. These lysates analyzed quantitative high-resolution electrophoresis on sulfate-polyacrylamide gels. This technique allowed detection and estimation molecular weight 15 virus-specific polypeptides: A, 100,000; B, 90,000; C, 84,000; D, 75,000, D1, 65,000; E, 56,000; e, 40,000; F, 38,000; α, 34,000; β, 30,000; γ, 23,000; G, 16,000; H, 12,000; I, 11,000; δ, 9,000. Pulse-chase experiments, conjunction cyanogen bromide tryptic mapping isolated polypeptides, indicate that at least three primary gene products (A,F,C), a cumulative about 220,000, are generated during translation RNA genome. Chains A C then undergo post-translational cleavages, while F remains uncleaved. The cleavage include capsid chains (α, e). Those D E. 230,000, stable produced equimolar amounts. model for of, sequence accounts for, polypeptides is proposed.