Vanadate oligomers interactions with myosin

‘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