Patzelt-Wenczler R, Schoner W
Biochim Biophys Acta. 1975 Oct 22;403(2):538-43. doi: 10.1016/0005-2744(75)90082-0.
(Na+ + K+)-activated ATPase in beef brain microsomes is inactivated by the disulfide of thionosine tri[gamma-32P]phosphate, an ATP analog. The inactivation of the enzyme, which is accompanied by an incorporation of radioactivity into the membrane protein, is abolished by ATP or dithiothreitol. Since dithiothreitol restores the activity of (Na+ + K+)-ATPase, which had previously been inactivated by this ATP analog, it is concluded that thionosine triphosphate disulfide reacts with a sulfhydryl group in the ATP binding site of (Na+ + K+)-activated ATPase.
牛肉脑微粒体中的(钠+钾)激活的ATP酶被三磷酸硫代肌苷(一种ATP类似物)的二硫化物失活。该酶的失活伴随着放射性掺入膜蛋白,ATP或二硫苏糖醇可消除这种失活。由于二硫苏糖醇可恢复先前被这种ATP类似物失活的(钠+钾)-ATP酶的活性,因此得出结论,三磷酸硫代肌苷二硫化物与(钠+钾)激活的ATP酶的ATP结合位点中的巯基发生反应。