Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1989-12-22
pubmed:abstractText
The immune blotting method using monoclonal antibodies to Ml protein showed protein Ml to migrate in several bands in polyacrylamide gel electrophoresis (PGE) of influenza A virus polypeptides. The heterogeneous distribution of Ml protein in PGE is due to the formation of aggregates: dimers, trimers, and polymers of a higher order. The capacity of Ml protein for aggregation is typical not of all influenza virus strains and most likely is not associated with gel overloading. Since dimers and trimers of Ml protein comigrate in the gel with virus-specific proteins such as NP and proteins of a polymerase complex, this circumstance should be take into consideration in using PGE for isolation of pure influenza virus proteins.
pubmed:language
rus
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0507-4088
pubmed:author
pubmed:issnType
Print
pubmed:volume
34
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
408-11
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:articleTitle
[Heterogeneous distribution of influenza A matrix protein in polyacrylamide gel, detected using an immunoblotting method with monoclonal antibodies].
pubmed:publicationType
Journal Article, English Abstract