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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 131-136 |
| Number of pages | 6 |
| Journal | Advances in experimental medicine and biology |
| Volume | 218 |
| DOIs | |
| State | Published - 1987 |
| Externally published | Yes |
ASJC Scopus subject areas
- Biochemistry, Genetics and Molecular Biology(all)
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Cite this
Hogue, B. G., & Brian, D. A. (1987). Glycosylation of the bovine coronavirus hemagglutinin protein. Advances in experimental medicine and biology, 218, 131-136. https://doi.org/10.1007/978-1-4684-1280-2_15