Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1992-4-13
pubmed:abstractText
The usefulness of a native gel electroblotting technique in the study of protein-protein interactions was demonstrated by the determination of the stoichiometry of the interaction between interleukin-2 (IL-2) and the alpha subunit of IL-2 receptor (IL-2R alpha) in solution. Complexes formed between the recombinant forms of the two proteins in solution were separated from the noncomplexed protein molecules by electrophoresis in a native polyacrylamide gel and the protein bands were electroblotted quantitatively onto polyvinyldiene difluoride membranes for further structural analysis. The data obtained from sequence and amino acid analyses of the blotted proteins provided direct evidence that IL-2 binds to IL-2R alpha in a 1:1 ratio. This methodology should be applicable to the study of other structure/function aspects of protein-protein interactions in solution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0003-2697
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
198
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
285-91
pubmed:dateRevised
2006-4-17
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Structural analyses of proteins electroblotted from native polyacrylamide gels onto polyvinyldiene difluoride membranes. A method for determining the stoichiometry of protein-protein interaction in solution.
pubmed:affiliation
Department of Protein Biochemistry, Hoffmann-La Roche Incorporated, Nutley, New Jersey 07110.
pubmed:publicationType
Journal Article