Sodium-potassium adenosine triphosphatase: acyl phosphate "intermediate" shown to be L-glutamyl-gamma-phosphate.
Peptides obtained from pepsin digestion of the phosphorylated and nonphosphorylated forms of a preparation of brain microsomal sodium-potassium-activated adenosine triphosphatase were treated at pH 5.4 with N-(n-propyl-2,3-(3)H) hydroxylamine of high specific activity, then separated by column chromatography, and further digested with pronase. A compound isolated in higher amounts from the phosphorylated enzyme than from the nonphosphorylated enzyme migrated with authentic L-glutamyl-gamma-propylhydroxamate in four chromatographic systems and on electrophoresis on paper at three different pH's. The acyl phosphate "intermediate" in the phosphorylated form of the adenosine-triphosphatase therefore appears to be an L-glutamyl-gamma-phosphate residue.
D000251:Adenosine Triphosphatases / Q000032:analysis*; D000818:Animals; D001921:Brain / Q000166:cytology / Q000201:enzymology*; D002845:Chromatography; D004586:Electrophoresis; D006168:Guinea Pigs; D006863:Hydrogen-Ion Concentration; D066298:In Vitro Techniques; D008861:Microsomes / Q000201:enzymology*; D010434:Pepsin A; D010455:Peptides / Q000032:analysis*; D010710:Phosphates / Q000032:analysis*
D010455:Peptides; D010710:Phosphates; D010434:Pepsin A; D000251:Adenosine Triphosphatases