The cytochemical demonstration of NaK dependent adenosine triphosphatase at electrocyte level in Eigenmannia virescens (Gymnotidae).
ATPase activity (E.C. 3.6.1.3.) has been studied by electron microscopy with the help of several cytochemical techniques on Eigenmannia virescens electrocytes. Incubation was carried out with in two different media containing paranitrophenyl phosphate (p-NPP) or adenosine triphosphate (ATP) as substrate. With p-NPP the phosphate freed is captured at alkaline pH, either by strontium chloride or by lead citrate. With ATP the phosphate freed is captured at a pH close to neutrality by the lead nitrate. NaK ATPase activity was only demonstrated with the medium containing ATP; the positive results obtained with this technique were sensitive to ouabain. The enzyme is situated both on the membrane of the posterior face which is innervated and on that of the anterior face of the electrocytes. The cytoplasm of the anterior face is occupied by a strong concentration of tubules on whose membranes the enzyme is also present. The localisation of the enzyme on the tubules can explain biochemical results which indicate that 70% of the total NaK ATPase of the electrolytes is situated at the level of the anterior face.
D000818:Animals; D002462:Cell Membrane / Q000201:enzymology; D004557:Electric Organ / Q000201:enzymology*; D005399:Fishes / Q000378:metabolism*; D006651:Histocytochemistry; D009596:Nitrophenols; D009943:Organophosphorus Compounds; D000254:Sodium-Potassium-Exchanging ATPase / Q000378:metabolism*
D009596:Nitrophenols; D009943:Organophosphorus Compounds; C008644:nitrophenylphosphate; D000254:Sodium-Potassium-Exchanging ATPase