title: Adenosine triphosphatase localization in the branchial heart appendage of Sepia officinalis L. (Cephalopoda).
abstract: Sodium- and potassium-dependent adenosine triphosphatase (Na+--K+-ATPase) has been demonstrated in the branchial heart appendage (pericardial gland) of Sepia officinalis L. by biochemical, cytochemical and autoradiographical methods. The biochemical data indicate the presence of Na+--K+-ATPase, judging from the potassium dependency and, with some restrictions, the inhibition by ouabain. Cytochemically and autoradiographically, the enzyme could be localized on the cytoplasmic surfaces of the lateral plasma membranes and the basal membrane infoldings (basal labyrinth) of the folded epithelium of the branchial heart appendage. The pdocytes of the peripheral zone of the organ reacted negatively. In addition to the Na+--K+-ATPase, a magnesium-activated adenosine triphosphatase (Mg2+-ATPase) was demonstrated in the folded epithelium, localized mainly in the mitochondria but also at the brush border and in the apical intercellular space, whereas a bicarbonate-stimulated ATPase (HCO-3-ATPase) was present only in the mitochondria.
mesh_terms: D000251:Adenosine Triphosphatases / Q000032:analysis; D000818:Animals; D001345:Autoradiography; D001639:Bicarbonates / Q000494:pharmacology; D004848:Epithelium / Q000201:enzymology; D006651:Histocytochemistry / Q000379:methods; D008274:Magnesium / Q000494:pharmacology; D008974:Mollusca / Q000201:enzymology*; D009206:Myocardium / Q000201:enzymology*; D000254:Sodium-Potassium-Exchanging ATPase / Q000032:analysis*; D013347:Subcellular Fractions / Q000201:enzymology; D014018:Tissue Distribution
chemical_list: D001639:Bicarbonates; D000251:Adenosine Triphosphatases; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium