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Direct or indirect influence of triphenyl-lead on activity of Na+/K+-ATPase

Stanis aw PrzestalskiDepartment of Physics and Biophysics, Agricultural University, Norwida 25, 50-375 Wrocław, PolandHalina Kleszczy skaDepartment of Physics and Biophysics, Agricultural University, Norwida 25, 50‐375 Wrocław, PolandZenon TrelaDepartment of Physics and Biophysics, Agricultural University, Norwida 25, 50-375 Wrocław, PolandZ. SpiakDepartment of Agricultural Chemistry, Agricultural University, Norwida 25, 50-375 Wrocław, PolandMaria ZamarajevaDepartment of Biology, Chair of Biophysics, Tashkent State University, 700095, Vuzgorodok, Tashkent, UzbekistanNatalia GlazyrinaDepartment of Biology, Chair of Biophysics, Tashkent State University, 700095, Vuzgorodok, Tashkent, UzbekistanA. I. Gagel’gansDepartment of Biology, Chair of Biophysics, Tashkent State University, 700095, Vuzgorodok, Tashkent, Uzbekistan
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Аннотация

We have studied the effect of triphenyl-lead chloride on the lipid phase of erythrocyte membranes, on lipid monomolecular layers and Na+/K+-ATPase of the microsomal fraction of rat brain. It was found that the haemolytic effect induced by this compound occurs when its concentration exceeds 30 µM. The minimal lead concentration inducing measurable effects in monomolecular lecithin layers is about 1 µM. Inhibition of Na+/K+-ATPase activity begins at a concentration exceeding 0.5 µM. Maximum inhibition is observed at around 40 µM—a concentration at which haemolysis also occurs. It can thus be thought that at very low lead concentrations the main (or exclusive) role in modifying membrane function is played by direct interaction between lead and the sulphydryl groups of ATPase, whereas at higher concentrations two effects seem to overlap: direct interaction between lead and enzymic proteins via their sulphydryl groups and as indirect influence on the proteins via changes in the organization of the lipid phase of the membrane. Copyright © 2000 John Wiley & Sons, Ltd.

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