Приказ основних података о документу
Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators
dc.creator | Krstić, Danijela Z. | |
dc.creator | Krinulović, Katarina | |
dc.creator | Vasić, Vesna M. | |
dc.date.accessioned | 2018-03-01T19:43:05Z | |
dc.date.available | 2018-03-01T19:43:05Z | |
dc.date.issued | 2005 | |
dc.identifier.issn | 1475-6366 | |
dc.identifier.uri | https://vinar.vin.bg.ac.rs/handle/123456789/2947 | |
dc.description.abstract | Kinetics and inhibition of Na+/K+-ATPase and Mg2+-ATPase activity from rat synaptic plasma membrane (SPM), by separate and simultaneous exposure to transition (Cu2+, Zn2+, Fe2+ and Co2+) and heavy metals (Hg(2+)and Pb2+) ions were studied. All investigated metals produced a larger maximum inhibition of Na+/K+-ATPase than Mg2+-ATPase activity. The free concentrations of the key species (inhibitor, MgATp(2-), MeATp(2-)) in the medium assay were calculated and discussed. Simultaneous exposure to the combinations Cu2+/Fe2+ or Hg2+/Pb(2+)caused additive inhibition, while Cu2+/Zn2+ or Fe2+/Zn2+ inhibited Na+/K+-ATPase activity synergistically (i.e., greater than the sum metal-induced inhibition assayed separately). Simultaneous exposure to Cu2+/Fe2+ or Cu2+/Zn2+ inhibited Mg2+-ATPase activity synergistically, while Hg2+/Pb2+ or Fe2+/Zn2+ induced antagonistic inhibition of this enzyme. Kinetic analysis showed that all investigated metals inhibited Na+/K+-ATPase activity by reducing the maximum velocities (V-max) rather than the apparent affinity (K-m) for substrate MgATp(2-), implying the noncompetitive nature of the inhibition. The incomplete inhibition of Mg2+-ATPase activity by Zn2+, Fe2+ and Co2+ as well as kinetic analysis indicated two distinct Mg2+-ATPase subtypes activated in the presence of low and high MgATp2- concentration. EDTA, L-cysteine and gluthathione (GSH) prevented metal ion-induced inhibition of Na+/K+-ATPase with various potencies. Furthermore, these ligands also reversed Na+/K+-ATPase activity inhibited by transition metals in a concentration-dependent manner, but a recovery effect by any ligand on Hg2+-induced inhibition was not obtained. | en |
dc.rights | restrictedAccess | en |
dc.source | Journal of Enzyme Inhibition and Medicinal Chemistry | en |
dc.subject | transition and heavy metals | en |
dc.subject | Na+/K+-ATPase | en |
dc.subject | Mg2+-ATPase | en |
dc.subject | kinetics | en |
dc.subject | inhibition | en |
dc.title | Inhibition of Na+/K+-ATPase and Mg2+-ATPase by metal ions and prevention and recovery of inhibited activities by chelators | en |
dc.type | article | en |
dcterms.abstract | Крстиц, Д; Кринуловиц, К; Васић Весна М; | |
dc.citation.volume | 20 | |
dc.citation.issue | 5 | |
dc.citation.spage | 469 | |
dc.citation.epage | 476 | |
dc.identifier.wos | 000233401700008 | |
dc.identifier.doi | 10.1080/14756360500213280 | |
dc.citation.rank | M22 | |
dc.identifier.pmid | 16335055 | |
dc.identifier.scopus | 2-s2.0-28244451280 |
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