Ultracytochemical characteristic of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase (Na(+)-K(+)-ATPase) of rat myocardium.
The ultracytochemical localization of ouabain-sensitive, potassium-dependent p-nitrophenylphosphatase within a rat heart has been studied. Our cytochemical procedure for the detection of enzyme activity is based on an incubation medium consisting of tris-maleate buffer, p-nitrophenylphosphate (p-NPP) as a substrate, lead nitrate as a trapping agent, MgCl2, KCl, levamisole, final pH = 7.3. The physiological pH of the incubation medium highly increases the authenticity of the enzymatic reaction and is the main advantage of the technique. Postincubation processing of specimens by 0.1 mol/l tris-maleate buffer pH = 6.0 confirms the specificity of the reaction and removes nonspecific precipitation.
Kiselyova
A P
AP
Department of Pathological Anatomy, Kiev Medical Institute, USSR.
Zinchuk
V S
VS
D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000818:Animals; D006651:Histocytochemistry; D007202:Indicators and Reagents; D008297:Male; D008854:Microscopy, Electron; D009206:Myocardium / Q000201:enzymology* / Q000648:ultrastructure; D010042:Ouabain / Q000494:pharmacology*; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D007202:Indicators and Reagents; D010042:Ouabain; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D000254:Sodium-Potassium-Exchanging ATPase