Abstract
Brush-border membrane vesicles (BBMV) from rat, rabbit and pig kidneys have been used to characterize renal ecto-ATPases. In rat1,2 and rabbit renal BBMV3, Mg2+ stimulated enzyme activity better than Ca2+, whereas in vesicles from pig kidney the reverse order was found.4,5 The ecto-ATPases from all species hydrolysed purine and pyrimidine nucleotides with ITP being the most effectively cleaved substrate in rat and rabbit renal BBMV,1, 2, 6 and ATP in porcine renal BBMV.5 In most studies, the Km for ATP was found in the range between 0.14 and and 0.4 mM.2–4, 6, 7 Vanadate, ouabain, azide, oligomycin, N-ethylmaleimide, and bafilomycin hardly decreased the activity of renal ecto-ATPases in concentrations sufficient to block ion-transporting ATPases.1, 3, 5 Here we report on the inhibition by Ca2+ channel blockers and phenothiazines as well as on the differential effect of Ca2+ and Mg2+ on the ecto-ATP diphosphohydrolase in pig kidney BBMV.
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Rengelshausen, J., Schweickhardt, C., Burckhardt, G. (1997). Inhibition of Porcine Renal Ecto-ATP Diphosphohydrolase by Ca2+ Channel Blockers and Neuroleptic Drugs. In: Plesner, L., Kirley, T.L., Knowles, A.F. (eds) Ecto-ATPases. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5955-9_13
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DOI: https://doi.org/10.1007/978-1-4615-5955-9_13
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