Partial purification and properties of (Na+ + K+)-ATPase from Potamon potamios.
1. The tissue distribution of the (Na+ + K+)-ATPase in the freshwater/land crab Potamon Potamios was studied. 2. Gills were found to display the highest total activity in the whole animal (47%) but the highest specific activity was detected in the heart (15.15 mumol Pi/mg protein/min). 3. All other organs tested were found to have low enzyme activity. 4. The freshwater/land crab ATPase enzyme was inhibited by ouabain with a Ki of 0.5 mM.Km values for ATP, Mg2+ and K+ were 1.4, 4.0 and 1.2 mM respectively. The enzyme also showed a break in the Arrhenius plot at 23 degrees C. 5. A purification method of microsomal ATPase is described involving ultracentrifugation and electrofocusing.
Institute of Molecular Biology and Biotechnology, Research Center of Crete, Heraklion, Greece.
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D000818:Animals; D003386:Brachyura / Q000201:enzymology*; D004591:Electrophoresis, Polyacrylamide Gel; D004795:Enzyme Stability / Q000502:physiology; D005880:Gills / Q000201:enzymology; D007700:Kinetics; D008297:Male; D008854:Microscopy, Electron; D008861:Microsomes / Q000201:enzymology; D000254:Sodium-Potassium-Exchanging ATPase / Q000737:chemistry / Q000302:isolation & purification*
D000254:Sodium-Potassium-Exchanging ATPase