Effects of lead and other inhibitors on the activation of K+-dependent p-nitrophenylphosphatase activity by glycine.
The in vitro and in vivo effects of lead on the activation of K+-dependent p-nitrophenylphosphatase activity by glycine were investigated in plasma membranes of male Wistar rat livers. This activation was markedly inhibited by lead in vitro (0.1-5.0 mM) and in vivo (intraperitoneal injection of lead at 4, 8, or 20 mg per 100 g body weight). On the other hand, the in vitro activation of this K+-dependent activity by glycine was about 77% inhibited by ouabain (10 micronM), but about 100% inhibited by oligomycin (20 micronM).
D009597:4-Nitrophenylphosphatase / Q000037:antagonists & inhibitors* / Q000378:metabolism; D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004789:Enzyme Activation / Q000187:drug effects; D005998:Glycine / Q000494:pharmacology*; D007854:Lead / Q000494:pharmacology*; D008099:Liver / Q000166:cytology; D008297:Male; D008930:Mitochondria, Liver / Q000201:enzymology; D009840:Oligomycins / Q000494:pharmacology; D010042:Ouabain / Q000494:pharmacology; D010744:Phosphoric Monoester Hydrolases / Q000037:antagonists & inhibitors*; D011188:Potassium / Q000494:pharmacology*; D011506:Proteins / Q000378:metabolism; D051381:Rats
D009840:Oligomycins; D011506:Proteins; D007854:Lead; D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D011188:Potassium; D005998:Glycine