Influence of triethyl lead on the activity of enzymes of the ascites tumor cell plasma membrane and its microviscosity.
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.
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
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