Localization of ouabain-sensitive, potassium-dependent nitrophenyl phosphatase in the rectal gland of the spiny dogfish, Squalus acanthias.
Tissue from the digitiform rectal gland of the spiny dogfish, Squalus acanthias, was fixed briefly by formaldehyde perfusion and studied for the specificity and localization of p-nitrophenyl phosphatase (NPP'ase) activity. The enzymatic activity was K+-dependent (56%) and ouabain-sensitive (67%-inhibition). The electron-dense reaction product (SrPO4) of the cytochemical reaction (Ernst, 1972b) was localized along the inner surfaces of the basolateral membranes of the secretory cells. It was absent from mitochondria nuclei, vesicles, and other organelles. The luminal surface of the secretory cells was slightly reactive. On the basis of (1) this pattern of localization for the sodium transport system, (2) the presence of extensive intercellular labyrinthine channels (Bulger, 1963) that would facilitate "standing gradients" (Diamond and Bossert, 1968), and (3) the specific distribution of the energy-providing mitochondria, we conclude that the concentration and electrochemical gradients recorded from the secreting gland (Hayslett et al., 1974) are maintained across the domains of the basolateral surfaces of the secretory cells.
D009597:4-Nitrophenylphosphatase / Q000032:analysis*; D000818:Animals; D001693:Biological Transport, Active; D002462:Cell Membrane / Q000201:enzymology; D004284:Dogfish / Q000378:metabolism*; D005260:Female; D006651:Histocytochemistry; D008854:Microscopy, Electron; D010744:Phosphoric Monoester Hydrolases / Q000032:analysis*; D012491:Salt Gland / Q000201:enzymology* / Q000648:ultrastructure; D012754:Sharks / Q000378:metabolism*; D012964:Sodium / Q000378:metabolism
D012964:Sodium; D010744:Phosphoric Monoester Hydrolases; D009597:4-Nitrophenylphosphatase