The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes
Abstract
The influence of transition metal (Cu2-,Zn2+, Fe2+ and Co2+) and heavy metal ions (Hg2+, Ph2+ and Cd2+) on the activities of Na+/K+-ATPase and Mg2+-ATPase isolated from rat synaptic plasma membranes (SPM) was investigated. The aim of the study was to elucidate the inhibition of both ATPase activities by exposure to the considered metal ions as a function of their affinity to bind to the -SH containing ligand L-cysteine, as a model system. The half-maximum inhibitory activities (IC50) of the enzymes were determined as parameters of rectangular hyperbolas and correlated with the stability constant (K-s) of the respective metal-ion-L-cysteine complex. The linear Dixon plots indicate equilibrium binding of the investigated ions to both enzymes.
Keywords:
transition metal ions / heavy metal ions / Na-/K(-)ATPase / Mg2+-ATPase / inhibitionSource:
Journal of the Serbian Chemical Society, 2004, 69, 7, 541-547
DOI: 10.2298/JSC0407541V
ISSN: 0352-5139
WoS: 000222831500004
Scopus: 2-s2.0-31544439395
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VinčaTY - JOUR AU - Vujisić Lj. AU - Krstić, Danijela Z. AU - Krinulović, Katarina AU - Vasić, Vesna M. PY - 2004 UR - https://vinar.vin.bg.ac.rs/handle/123456789/2789 AB - The influence of transition metal (Cu2-,Zn2+, Fe2+ and Co2+) and heavy metal ions (Hg2+, Ph2+ and Cd2+) on the activities of Na+/K+-ATPase and Mg2+-ATPase isolated from rat synaptic plasma membranes (SPM) was investigated. The aim of the study was to elucidate the inhibition of both ATPase activities by exposure to the considered metal ions as a function of their affinity to bind to the -SH containing ligand L-cysteine, as a model system. The half-maximum inhibitory activities (IC50) of the enzymes were determined as parameters of rectangular hyperbolas and correlated with the stability constant (K-s) of the respective metal-ion-L-cysteine complex. The linear Dixon plots indicate equilibrium binding of the investigated ions to both enzymes. T2 - Journal of the Serbian Chemical Society T1 - The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes VL - 69 IS - 7 SP - 541 EP - 547 DO - 10.2298/JSC0407541V ER -
@article{ author = "Vujisić Lj. and Krstić, Danijela Z. and Krinulović, Katarina and Vasić, Vesna M.", year = "2004", abstract = "The influence of transition metal (Cu2-,Zn2+, Fe2+ and Co2+) and heavy metal ions (Hg2+, Ph2+ and Cd2+) on the activities of Na+/K+-ATPase and Mg2+-ATPase isolated from rat synaptic plasma membranes (SPM) was investigated. The aim of the study was to elucidate the inhibition of both ATPase activities by exposure to the considered metal ions as a function of their affinity to bind to the -SH containing ligand L-cysteine, as a model system. The half-maximum inhibitory activities (IC50) of the enzymes were determined as parameters of rectangular hyperbolas and correlated with the stability constant (K-s) of the respective metal-ion-L-cysteine complex. The linear Dixon plots indicate equilibrium binding of the investigated ions to both enzymes.", journal = "Journal of the Serbian Chemical Society", title = "The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes", volume = "69", number = "7", pages = "541-547", doi = "10.2298/JSC0407541V" }
Vujisić Lj., Krstić, D. Z., Krinulović, K.,& Vasić, V. M.. (2004). The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes. in Journal of the Serbian Chemical Society, 69(7), 541-547. https://doi.org/10.2298/JSC0407541V
Vujisić Lj., Krstić DZ, Krinulović K, Vasić VM. The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes. in Journal of the Serbian Chemical Society. 2004;69(7):541-547. doi:10.2298/JSC0407541V .
Vujisić Lj., Krstić, Danijela Z., Krinulović, Katarina, Vasić, Vesna M., "The influence of transition and heavy metal ions on ATP-ases activity in rat synaptic plasma membranes" in Journal of the Serbian Chemical Society, 69, no. 7 (2004):541-547, https://doi.org/10.2298/JSC0407541V . .