Glycosylation of the bovine coronavirus hemagglutinin protein.

B. G. Hogue; D. A. Brian

doi:10.1007/978-1-4684-1280-2_15

Glycosylation of the bovine coronavirus hemagglutinin protein.

B. G. Hogue, D. A. Brian

Research output: Contribution to journal › Article › peer-review

1 Scopus citations

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	https://doi.org/10.1007/978-1-4684-1280-2_15
State	Published - 1987
Externally published	Yes

ASJC Scopus subject areas

Biochemistry, Genetics and Molecular Biology(all)

Access to Document

10.1007/978-1-4684-1280-2_15

Fingerprint Dive into the research topics of 'Glycosylation of the bovine coronavirus hemagglutinin protein.'. Together they form a unique fingerprint.

Cite this

@article{99d4f94134594811b379e7998817c4b9,

title = "Glycosylation of the bovine coronavirus hemagglutinin protein.",

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.",

author = "Hogue, {B. G.} and Brian, {D. A.}",

note = "Copyright: This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine",

year = "1987",

doi = "10.1007/978-1-4684-1280-2_15",

language = "English (US)",

volume = "218",

pages = "131--136",

journal = "Advances in Experimental Medicine and Biology",

issn = "0065-2598",

publisher = "Springer New York",

}

TY - JOUR

T1 - Glycosylation of the bovine coronavirus hemagglutinin protein.

AU - Hogue, B. G.

AU - Brian, D. A.

N1 - Copyright: This record is sourced from MEDLINE/PubMed, a database of the U.S. National Library of Medicine

PY - 1987

Y1 - 1987

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=0023494064&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023494064&partnerID=8YFLogxK

U2 - 10.1007/978-1-4684-1280-2_15

DO - 10.1007/978-1-4684-1280-2_15

M3 - Article

C2 - 3124516

AN - SCOPUS:0023494064

VL - 218

SP - 131

EP - 136

JO - Advances in Experimental Medicine and Biology

JF - Advances in Experimental Medicine and Biology

SN - 0065-2598

ER -

Glycosylation of the bovine coronavirus hemagglutinin protein.

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this