<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="6.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Tiago, T.</style></author><author><style face="normal" font="default" size="100%">Aureliano, M.</style></author><author><style face="normal" font="default" size="100%">Duarte, R. O.</style></author><author><style face="normal" font="default" size="100%">Moura, J. J. G.</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Vanadate oligomers interaction with phosphorylated myosin</style></title><secondary-title><style face="normal" font="default" size="100%">Inorganica Chimica Acta</style></secondary-title></titles><dates><year><style  face="normal" font="default" size="100%">2002</style></year><pub-dates><date><style  face="normal" font="default" size="100%">Nov 15</style></date></pub-dates></dates><urls><web-urls><url><style face="normal" font="default" size="100%">http://dx.doi.org/10.1016/s0020-1693(02)00948-9</style></url></web-urls></urls><volume><style face="normal" font="default" size="100%">339</style></volume><pages><style face="normal" font="default" size="100%">317-321</style></pages><isbn><style face="normal" font="default" size="100%">0020-1693</style></isbn><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;Using a myosin preparation containing endogenous myosin light-chain (LC2) kinase and phosphatase and calmodulin, i.e. near physiological ones, the interaction of vanadate oligomers with phosphorylated myosin was evaluated. Decavanadate or metavanadate solutions (2-15 mM total vanadate) did not prevent the phosphorylation state of the regulatory myosin lightchain, as observed by urea-polyacrylamide gel electrophoresis. The relative order of line broadening upon protein addition, reflecting the interaction of the vanadate oligomers with phosphorylated myosin, was V10 &amp;gt; V-4 &amp;gt; V-1 = 1 whereas, no changes were observed for monomeric vanadate. In the presence of ATP, V-1 signal was shifted upfield 2 ppm and became broadened, while V4 signal became narrowed. Moreover, a significant increase in myosin ATPase inhibition (60%) was observed when decameric vanadate species were present (1.4 mM). It is concluded that, under conditions near physiological ones, decameric vanadate differs from vanadate oligomers present in metavanadate solutions due to its strong interaction with the phosphorylated enzyme and myosin ATPase inhibition. Besides, ATP decreases the affinity of myosin for tetravanadate, induces the interaction with monomeric vanadate, whereas it does not affect decameric vanadate interaction. (C) 2002 Elsevier Science B.V. All rights reserved.&lt;/p&gt;
</style></abstract><accession-num><style face="normal" font="default" size="100%">WOS:000179281100039</style></accession-num><notes><style face="normal" font="default" size="100%">&lt;p&gt;Times Cited: 4&lt;/p&gt;
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