Abstract
The bovine coronavirus hemagglutinin protein gp140 is composed of disulfide-linked subunits of 65 kDa. This protein was further characterized with regard to its glycosylation. The glycosylated subunits of the protein are polypeptides having a molecular mass of 42.5 kDa. Both subunits appear to be processed to the same extent by the addition of N-linked oligosaccharides. Each subunit on the mature virion has 6–7 high mannose and 3–4 complex type carbohydrate chains attached to it.
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© 1987 Plenum Press, New York
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Hogue, B.G., Brian, D.A. (1987). Glycosylation of the Bovine Coronavirus Hemagglutinin Protein. In: Lai, M.M.C., Stohlman, S.A. (eds) Coronaviruses. Advances in Experimental Medicine and Biology, vol 218. Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-1280-2_15
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DOI: https://doi.org/10.1007/978-1-4684-1280-2_15
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