[Isolation and properties of anion-sensitive adenosine triphosphatase from erythrocyte membranes].
Using the non-ionic detergent Triton X-100 and gel-chromatography, an anion-sensitive ATPase was isolated from rat and rabbit erythrocyte membranes. The ATPase preparations possess no Na, K- or Mg, Ca-ATPase activities. ATPase from rat erythrocyte membranes is made up of five subunits with molecular weights of 58 000 (alpha), 50 000 (beta), 36 000 (gamma), 25 000 (delta) and 12 000 (epsilon) and can be represented by the formula alpha 3 beta 3 gamma delta epsilon.
D000251:Adenosine Triphosphatases / Q000097:blood* / Q000302:isolation & purification; D000818:Animals; D000838:Anions; D003902:Detergents; D004910:Erythrocyte Membrane / Q000201:enzymology*; D004912:Erythrocytes / Q000201:enzymology*; D046911:Macromolecular Substances; D008970:Molecular Weight; D017830:Octoxynol; D011092:Polyethylene Glycols; D011817:Rabbits; D051381:Rats
D000838:Anions; D003902:Detergents; D046911:Macromolecular Substances; D011092:Polyethylene Glycols; D017830:Octoxynol; D000251:Adenosine Triphosphatases
Vydelenie i svoĭstva anionchuvstvitel'noĭ adenozintrifosfatazy iz membran éritrotsitov.