Kahlenberg A, Galsworthy P R, Hokin L E
Science. 1967 Jul 28;157(3787):434-6. doi: 10.1126/science.157.3787.434.
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.
从脑微粒体钠钾激活的三磷酸腺苷酶制剂的磷酸化和非磷酸化形式经胃蛋白酶消化得到的肽段,在pH 5.4下用高比活性的N-(正丙基-2,3-(3)H)羟胺处理,然后通过柱色谱分离,再用链霉蛋白酶进一步消化。从磷酸化酶中分离出的一种化合物比从非磷酸化酶中分离出的量更多,在四种色谱系统以及在三种不同pH值下的纸上电泳中,它与纯L-谷氨酰-γ-丙基羟肟酸迁移情况相同。因此,三磷酸腺苷酶磷酸化形式中的酰基磷酸“中间体”似乎是一个L-谷氨酰-γ-磷酸残基。