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ID 30521
JaLCDOI
FullText URL
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Author
Ueba, Osamu
Abstract

Treatment of respiratory syncytial (RS) virus with Triton X-100 in solutions of low ionic strength solubilized not only glycoproteins but also some non-glycosylated proteins. Rate zonal sedimentation of the solubilized materials resulted in separation of the glycoproteins from the other components, i.e. one fraction predominantly composed of two glycoproteins each with molecular weight (mol. wt.) of approximately 100,000 and 53,000 was obtained. Electron microscopic observation of this fraction revealed numerous club- or rod-shaped fine structures, suggesting that these were spikes of RS virus. After removal of Triton X-100 the structures aggregated and formed oligomers and polymers.

Keywords
respiratory syncytial virus
spike glycoproteins.
Amo Type
Article
Publication Title
Acta Medica Okayama
Published Date
1980-09
Volume
volume34
Issue
issue4
Publisher
Okayama University Medical School
Start Page
245
End Page
254
ISSN
0386-300X
NCID
AA00508441
Content Type
Journal Article
language
English
File Version
publisher
Refereed
True
PubMed ID
Web of Science KeyUT