| Literature DB >> 6310152 |
A A Thomas, H O Voorma, A Boeye.
Abstract
Poliovirus proteinase was studied in vitro in lysates from poliovirus-infected HeLa cells. Preincubation of these lysates caused (i) a reduction in poliovirus proteinase activity and (ii) a partial dependence on exogenous mRNA for optimal translation. Proteins translated from endogenous poliovirus RNA in preincubated extracts from virus-infected HeLa cells are poorly cleaved. This cleavage deficiency is alleviated by adding fresh poliovirus RNA to the translation system, thus, allowing re-initiation to occur. This suggests that the poliovirus proteinase is highly unstable.Entities:
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Year: 1983 PMID: 6310152 PMCID: PMC255348
Source DB: PubMed Journal: J Virol ISSN: 0022-538X Impact factor: 5.103