Ultrastructural demonstration of alkaline phosphatase (ALP) and K+-p-nitrophenyl phosphatase (K+-p-NPPase) in the epidermal ionocytes of Blennius sanguinolentus.
Cytochemical techniques were used for the light and electron microscopical localization of alkaline phosphatase and potassium-dependent nitrophenyl phosphatase in the epidermal ionocytes of the Teleost Blennius sanguinolentus. The heavier deposition of the reaction products obtained with the different media was shown in the cytoplasmic surface of the labyrinth tubules, the apical vesicles and in intimate association with plasmic membranes. Both plasma membranes and intracellular activities are affected by the addition of specific inhibitors L-p-bromotetramisole oxalate and ouabain) to both complete and control media. The significance of the cytoplasmic localization of both the two enzymes is discussed with reference to current models of transepithelial ion transportation.
D009597:4-Nitrophenylphosphatase / Q000378:metabolism*; D000469:Alkaline Phosphatase / Q000378:metabolism*; D000818:Animals; D003593:Cytoplasm / Q000201:enzymology / Q000648:ultrastructure; D004817:Epidermis / Q000201:enzymology* / Q000648:ultrastructure; D005399:Fishes / Q000378:metabolism*; D006651:Histocytochemistry; D008854:Microscopy, Electron; D010744:Phosphoric Monoester Hydrolases / Q000378:metabolism*; D011188:Potassium / Q000378:metabolism*
D000469:Alkaline Phosphatase; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase; D011188:Potassium