Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1989-8-3
pubmed:abstractText
Bovine herpesvirus type 4 proteins were identified by PAGE of [35S]methionine- or [3H]glucosamine-labelled purified virions. Thirty-one monoclonal antibodies (MAbs) raised against the V. Test strain were used to identify 29 proteins, ten of which were glycosylated. All of these glycoproteins belonged to the viral envelope and a 140K non-glycosylated protein appeared to be the major nucleocapsid protein. The MAbs were classified into two groups. The first group precipitated three glycoproteins of Mr 150K, 120K and 51K. The 120K and 51K glycoproteins were linked by disulphide bonds and the 150K glycoprotein was linked to the others by non-covalent bonds. The second group precipitated a different 120K glycoprotein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0022-1317
pubmed:author
pubmed:issnType
Print
pubmed:volume
70 ( Pt 7)
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1743-53
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1989
pubmed:articleTitle
Proteins specified by bovine herpesvirus type 4: structural proteins of the virion and identification of two major glycoproteins by using monoclonal antibodies.
pubmed:affiliation
Department of Virology-Immunology, Faculty of Veterinary Medicine, University of Liège, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't