Solubilization and separation of divalent cation dependent adenosinetriphosphatase in native gradient polyacrylamide slab gel.
A new method for the simultaneous solubilization and separation of different cation dependent adenosinetriphosphatases after non-denaturing polyacrylamide gel electrophoresis is described. Using a gradient system, 3 distinct divalent cation dependent adenosinetriphosphatase bands (Mg2+-, Ca2+-, and Mg2+ + Ca2+-dependent) could be separated on the same gel from NP-40 solubilized brain microsomal preparations. This indicates that these 3 adenosinetriphosphatases represent distinct molecular species.
D000818:Animals; D001921:Brain / Q000201:enzymology*; D000252:Calcium-Transporting ATPases / Q000302:isolation & purification*; D002540:Cerebral Cortex / Q000201:enzymology; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods*; D008274:Magnesium; D008861:Microsomes / Q000201:enzymology; D051381:Rats; D000254:Sodium-Potassium-Exchanging ATPase / Q000302:isolation & purification*; D012995:Solubility
D000252:Calcium-Transporting ATPases; D000254:Sodium-Potassium-Exchanging ATPase; D008274:Magnesium