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Vanadate oligomers interactions with myosin

dc.contributor.authorAureliano, M.
dc.date.accessioned2014-07-15T09:22:38Z
dc.date.available2014-07-15T09:22:38Z
dc.date.issued2000
dc.description.abstract‘Monovanadate’containingamixtureofatleastfourdifferentvanadatespeciesand‘decavanadate’containingapparentlyonlytwovanadate species, mainly decameric species, inhibit myosin and actomyosin ATPase activities. The addition of myosin to ‘monovanadate’ and ‘decavanadate’solutionspromotesdifferentialincreasesonthe 51VNMRspectrallinewidthsofvanadateoligomers.Therelativeorderofline broadening upon myosin addition, reflecting the interaction of the vanadate oligomers with the protein, wasV10)V4)V1s1,whereas no changes were observed for monomeric vanadate species.It is concluded that decameric and tetrameric vanadate species interact quite potently with the protein and affect myosin as well actomyosin ATPase activities.por
dc.identifier.doihttp://dx.doi.org/ 10.1016/S0162-0134(00)00021-0
dc.identifier.issn0162-0134
dc.identifier.otherAUT: MAA01296;
dc.identifier.urihttp://hdl.handle.net/10400.1/4775
dc.language.isoengpor
dc.peerreviewedyespor
dc.publisherElsevierpor
dc.relation.publisherversionhttp://www.sciencedirect.com/science/article/pii/S0162013400000210por
dc.subjectVanadatepor
dc.subjectMyosinpor
dc.titleVanadate oligomers interactions with myosinpor
dc.typejournal article
dspace.entity.typePublication
oaire.citation.endPage143por
oaire.citation.issue1-2por
oaire.citation.startPage141por
oaire.citation.titleJournal of Inorganic Biochemistrypor
oaire.citation.volume80por
person.familyNameAureliano
person.givenNameManuel
person.identifier584146
person.identifier.ciencia-idAA14-3490-DC5E
person.identifier.orcid0000-0003-4858-3201
person.identifier.ridI-3283-2012
person.identifier.scopus-author-id6603412860
rcaap.rightsrestrictedAccesspor
rcaap.typearticlepor
relation.isAuthorOfPublicationbb413661-7edd-4b57-8338-33889cfd05db
relation.isAuthorOfPublication.latestForDiscoverybb413661-7edd-4b57-8338-33889cfd05db

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