| Literature DB >> 3838336 |
E E Walsh, M W Brandriss, J J Schlesinger.
Abstract
The fusion protein of respiratory syncytial virus was purified by affinity chromatography using a monoclonal antibody. Under various conditions the protein was recovered as a 145K dimer or a 70K monomer. The 70K monomer was composed of disulphide-linked fragments of 48K and 23K. Polyclonal rabbit serum produced to the dimerized fusion protein neutralized virus but did not inhibit fusion, while rabbit serum to the 2-mercaptoethanol-treated dimerized protein neutralized virus and inhibited fusion of infected cells. Only the latter serum strongly recognized the 23K fragment when studied by Western blot analysis.Entities:
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Year: 1985 PMID: 3838336 DOI: 10.1099/0022-1317-66-3-409
Source DB: PubMed Journal: J Gen Virol ISSN: 0022-1317 Impact factor: 3.891