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Studies on the interaction between titin and myosin

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dc.contributor.authorWang, Seu-Meies
dc.contributor.authorChung-Jiuan Jenges
dc.contributor.authorMu-Chien Sun
dc.date.accessioned2011-02-01T08:47:20Z
dc.date.available2011-02-01T08:47:20Z
dc.date.issued1992
dc.description.abstractThis study examines the interaction of titin and mysoin. In order to analyze the domains of myosin contributing to the binding for titin, we conducted a solid phase binding assay. Different portions of mysoin (heavy chains, light chains and myosin fragments ) were coated on the microtiter wells and reacted with biotinylated titin. Then the binding of biotinylated titin to these polypeptides was detected by using the avidinbiotin- peroxidase method. The results demonstrated that light meromyosin and subfragment 1 were the major domains of myosin interacting with titin. Titin fragments obtained by trypsin digestion were allowed to react with myosin in an affinity column, and the bound fragments were isolated by an acidic elution. Immunoblot analysis of mysoin-bound titin fragments revealed that an A-band domain of titin was responsible for the binding of myosin. In addition, biotinylated titin labelled the outer A-bands and Z-bands in intact myofibrils, thus confirming the in situ binding of titin to myosin.es
dc.formatapplication/pdfes
dc.format.extent5es
dc.identifier.issn0213-3911es
dc.identifier.urihttp://hdl.handle.net/10201/18325
dc.languageenges
dc.publisherMurcia : F. Hernándezes
dc.relation.ispartofHistology and histopathologyes
dc.rightsinfo:eu-repo/semantics/openAccesses
dc.subjectTitines
dc.subjectMyosines
dc.subject.otherCDU::6 - Ciencias aplicadas::61 - Medicinaes
dc.titleStudies on the interaction between titin and myosines
dc.typeinfo:eu-repo/semantics/articlees
dspace.entity.typePublicationes
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Histology and histopathology Vol. 7, nº 3 (1992)