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dc.contributor.authorLuna, Elizabeth J.
dc.contributor.authorWang, Y. L.
dc.contributor.authorVoss, E. W. Jr.
dc.contributor.authorBranton, D.
dc.contributor.authorTaylor, D. L.
dc.date2022-08-11T08:11:04.000
dc.date.accessioned2022-08-23T17:31:33Z
dc.date.available2022-08-23T17:31:33Z
dc.date.issued1982-11-10
dc.date.submitted2007-11-13
dc.identifier.citationJ Biol Chem. 1982 Nov 10;257(21):13095-100.
dc.identifier.issn0021-9258 (Print)
dc.identifier.pmid7130194
dc.identifier.urihttp://hdl.handle.net/20.500.14038/50761
dc.description.abstractA high capacity F-actin affinity matrix is constructed by binding fluorescyl-actin to rabbit anti-fluorescein IgG that is covalently bound to Sepharose 4B. When stabilized with phalloidin, the actin remains associated with the Sepharose beads during repeated washes, activates the ATPase activity of myosin subfragment 1, and specifically binds 125I-heavy meromyosin and 125I-tropomyosin. The associations between the F-actin affinity matrix and the iodinated F-actin binding proteins are monitored both by affinity chromatography and by a rapid, low speed sedimentation assay. Anti-fluorescein IgG-Sepharose should be generally useful as a matrix for the immobilization of proteins containing accessible, covalently bound fluorescein groups.
dc.language.isoen_US
dc.relation<a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7130194&dopt=Abstract">Link to article in PubMed</a>
dc.relation.urlhttp://www.jbc.org/content/257/21/13095.full.pdf+html
dc.subject*Actins
dc.subjectAnimals
dc.subjectChromatography, Affinity
dc.subjectMicroscopy, Electron
dc.subjectMuscle Proteins
dc.subjectMuscles
dc.subjectRabbits
dc.subjectSepharose
dc.subjectSpectrometry, Fluorescence
dc.subjectCell Biology
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleA stable, high capacity, F-actin affinity column
dc.typeJournal Article
dc.source.journaltitleThe Journal of biological chemistry
dc.source.volume257
dc.source.issue21
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/wfc_pp/289
dc.identifier.contextkey392373
html.description.abstract<p>A high capacity F-actin affinity matrix is constructed by binding fluorescyl-actin to rabbit anti-fluorescein IgG that is covalently bound to Sepharose 4B. When stabilized with phalloidin, the actin remains associated with the Sepharose beads during repeated washes, activates the ATPase activity of myosin subfragment 1, and specifically binds 125I-heavy meromyosin and 125I-tropomyosin. The associations between the F-actin affinity matrix and the iodinated F-actin binding proteins are monitored both by affinity chromatography and by a rapid, low speed sedimentation assay. Anti-fluorescein IgG-Sepharose should be generally useful as a matrix for the immobilization of proteins containing accessible, covalently bound fluorescein groups.</p>
dc.identifier.submissionpathwfc_pp/289
dc.contributor.departmentDepartment of Cell Biology
dc.source.pages13095-100


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