Effects of lead and other inhibitors on the activation of K+-dependent p-nitrophenylphosphatase activity by glycine.
J Toxicol Environ Health, 1977/1;2(3):663-9.
PMID: 191632
Abstract
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).
MeSH terms
4-Nitrophenylphosphatase; Animals; Cell Membrane; Enzyme Activation; Glycine; Lead; Liver; Male; Mitochondria, Liver; Oligomycins; Ouabain; Phosphoric Monoester Hydrolases; Potassium; Proteins; Rats
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