Purification and characterization of the respiratory syncytial virus fusion protein
Clicks: 183
ID: 272831
1985
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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 se …
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| Authors | Walsh EE;Brandriss MW;Schlesinger JJ;; |
| Journal | the journal of general virology |
| Year | 1985 |
| DOI |
DOI not found
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| Keywords |
National Center for Biotechnology Information
NCBI
NLM
MEDLINE
humans
pubmed abstract
nih
national institutes of health
national library of medicine
research support
non-u.s. gov't
Antibodies
cell line
viral / immunology
viral envelope proteins / immunology
molecular weight
e e walsh
respiratory syncytial viruses / analysis*
viral fusion proteins
j j schlesinger
m w brandriss
viral envelope proteins / isolation & purification*
amino acids / analysis
pmid:3838336
doi:10.1099/0022-1317-66-3-409
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