Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1993-5-27
pubmed:abstractText
Two kinds of unrelated African swine fever virus proteins of 220 kDa have been identified by means of two-dimensional gel electrophoresis and immunoprecipitation analysis. One species, named pp220 and identified as the precursor of the major structural protein p150, was found to be a moderately acidic protein (pl near 7) expressed after the replication of the viral DNA. The second species, a cluster of 220-kDa proteins with slightly different isoelectric points (pl ranging from 5 to 6), was found to be a homooligomeric complex formed by an early 32-kDa protein. This component was identified as the viral phosphoprotein p32, the most immunogenic early protein of African swine fever virus. A detailed characterization of its oligomeric structure is reported.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
194
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
284-93
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Characterization of two African swine fever virus 220-kDa proteins: a precursor of the major structural protein p150 and an oligomer of phosphoprotein p32.
pubmed:affiliation
Centro de Biología Molecular (C.S.I.C.-U.A.M.), Facultad de Ciencias, Universidad Autónoma, Cantoblancó, Madrid, Spain.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't