Ca2+-dependent phosphatase and ATPase activities in eel gill plasma membranes--I. Identification of Ca2+-activated ATPase activities with non-specific phosphatase activities.
The characteristics of Ca2+-activated ATPase activities previously often postulated as components for the calcium transporting system in fish gills do not fulfil the requirements of a transport Ca2+-ATPase. The chelation of Ca2+- or Mg2+-ions is a prerequisite for the adenosinephosphate esters to serve as substrate for gill plasma membrane phosphatases. Ca2+-activated ATP hydrolysis results from the activity of a heterogeneous pool of phosphatases located in the plasma membranes of the branchial epithelium, as is concluded from substrate specificity tests and the effects of various inhibitors on these hydrolytic activities. In the present study only non-specific phosphatases could be shown.
D000227:Adenine Nucleotides / Q000378:metabolism; D000811:Anguilla / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D000252:Calcium-Transporting ATPases / Q000037:antagonists & inhibitors / Q000378:metabolism*; D002462:Cell Membrane / Q000201:enzymology; D004355:Drug Stability; D005260:Female; D005880:Gills / Q000201:enzymology*; D007700:Kinetics; D008274:Magnesium / Q000494:pharmacology; D013379:Substrate Specificity
D000227:Adenine Nucleotides; D000252:Calcium-Transporting ATPases; D008274:Magnesium; D002118:Calcium