Linked Life Data

3824906

Source:http://linkedlifedata.com/resource/pubmed/id/3824906

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1987-4-3
pubmed:abstractText
The fusion protein of canine distemper virus was isolated by immunoadsorption from two virus strains, the rapidly growing Onderstepoort strain (forming large plaques) and the Convac vaccine strain (forming microplaques). The F1 subunits of the two fusion proteins were purified by preparative polyacrylamide gel electrophoresis. Direct amino acid sequence analysis revealed that 36-residue N-terminal regions of the proteins from the two strains are identical except at position 9, where Ala in the Convac strain is substituted by Val in the Onderstepoort strain. The two sequences show high homology with the previously determined N-terminal sequence of the F1 polypeptide of measles virus, and moderate homology with corresponding sequences of five paramyxoviruses, emphasizing the occurrence of an extensive conservation of these structures.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
157
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
241-4
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
F1 polypeptides of two canine distemper virus strains: variation in the conserved N-terminal hydrophobic region.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't