Coupling tandem affinity purification and quantitative tyrosine iodination to determine subunit stoichiometry of protein complexes
dc.contributor.author | Smith, Corey Lewis | |
dc.contributor.author | Peterson, Craig L. | |
dc.date | 2022-08-11T08:08:48.000 | |
dc.date.accessioned | 2022-08-23T16:08:55Z | |
dc.date.available | 2022-08-23T16:08:55Z | |
dc.date.issued | 2003-08-02 | |
dc.date.submitted | 2009-01-12 | |
dc.identifier.citation | <p>Methods. 2003 Sep;31(1):104-9.</p> | |
dc.identifier.issn | 1046-2023 (Print) | |
dc.identifier.doi | 10.1016/S1046-2023(03)00094-X | |
dc.identifier.pmid | 12893180 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/32565 | |
dc.description.abstract | Rapid protein purification methodologies, such as strategies involving the tandem affinity purification module, have resulted in the identification of a tremendous number of multisubunit protein complexes. Furthermore, in this modern genomic age, mass spectrometry methods are often coupled with affinity purification to identify the genes that encode each protein subunit. However, simple methodologies to determine the stoichiometry of individual subunits within a multisubunit complex have not received much attention. In this article we describe a procedure to rapidly and efficiently determine the stoichiometry of subunits within multisubunit complexes using a combination of tandem affinity purification and quantitative 125I labeling of subunit tyrosines. | |
dc.language.iso | en_US | |
dc.relation | <p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=12893180&dopt=Abstract">Link to Article in PubMed</a></p> | |
dc.relation.url | https://doi.org/10.1016/S1046-2023(03)00094-X | |
dc.subject | Electrophoresis, Polyacrylamide Gel; Fungal Proteins; Indicators and Reagents; Iodine Radioisotopes; Kinetics; Polymerase Chain Reaction; Radioisotope Dilution Technique; Tyrosine; Yeasts | |
dc.subject | Life Sciences | |
dc.subject | Medicine and Health Sciences | |
dc.title | Coupling tandem affinity purification and quantitative tyrosine iodination to determine subunit stoichiometry of protein complexes | |
dc.type | Journal Article | |
dc.source.journaltitle | Methods (San Diego, Calif.) | |
dc.source.volume | 31 | |
dc.source.issue | 1 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/gsbs_sp/1129 | |
dc.identifier.contextkey | 692121 | |
html.description.abstract | <p>Rapid protein purification methodologies, such as strategies involving the tandem affinity purification module, have resulted in the identification of a tremendous number of multisubunit protein complexes. Furthermore, in this modern genomic age, mass spectrometry methods are often coupled with affinity purification to identify the genes that encode each protein subunit. However, simple methodologies to determine the stoichiometry of individual subunits within a multisubunit complex have not received much attention. In this article we describe a procedure to rapidly and efficiently determine the stoichiometry of subunits within multisubunit complexes using a combination of tandem affinity purification and quantitative 125I labeling of subunit tyrosines.</p> | |
dc.identifier.submissionpath | gsbs_sp/1129 | |
dc.contributor.department | Program in Gene Function and Expression | |
dc.contributor.department | Program in Molecular Medicine | |
dc.contributor.department | Graduate School of Biomedical Sciences | |
dc.source.pages | 104-9 |