title: Influence of triethyl lead on the activity of enzymes of the ascites tumor cell plasma membrane and its microviscosity.
abstract: The influence of triethyl lead (TriEL) on the activity of plasma membrane-bound enzymes of Ehrlich ascites tumor cells and on membrane fluidity has been investigated. TriEL completely inhibits the (Na+-K+)-ATPase in its membrane-bound and even more pronounced in its solubilized form between 5 and about 20 microM. It also alters the microviscosity of the isolated plasma membrane up to a temperature of about 30 degrees C, but it does not have any influence on the fluidity of the membrane-derived liposomes. From these data it is concluded that the inhibitor may interact directly with the catalytic subunit of the (Na+ + K+)-ATPase, and may not exert its influence by interfering with the membrane lipids.
mesh_terms: D015720:5'-Nucleotidase; D000251:Adenosine Triphosphatases / Q000378:metabolism; D000469:Alkaline Phosphatase / Q000378:metabolism; D000818:Animals; D017301:Ca(2+) Mg(2+)-ATPase; D002286:Carcinoma, Ehrlich Tumor / Q000201:enzymology*; D002462:Cell Membrane / Q000201:enzymology*; D005454:Fluorescence Polarization; D007700:Kinetics; D007854:Lead / Q000633:toxicity*; D008560:Membrane Fluidity / Q000187:drug effects*; D051379:Mice; D009708:Nucleotidases / Q000378:metabolism; D009942:Organometallic Compounds / Q000633:toxicity*; D000254:Sodium-Potassium-Exchanging ATPase / Q000037:antagonists & inhibitors; D014783:Viscosity
chemical_list: D009942:Organometallic Compounds; D007854:Lead; C010360:triethyllead; D009708:Nucleotidases; D000469:Alkaline Phosphatase; D015720:5'-Nucleotidase; D000251:Adenosine Triphosphatases; D017301:Ca(2+) Mg(2+)-ATPase; D000254:Sodium-Potassium-Exchanging ATPase