Goto A, Yamada K, Ishii M, Yoshioka M, Ishiguro T, Eguchi C, Sugimoto T
Second Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
Biochem Biophys Res Commun. 1988 Aug 15;154(3):847-53. doi: 10.1016/0006-291x(88)90217-3.
We were able to purify a digitalis-like factor to apparent homogeneity from human urine based on the inhibitory effect on [3H]-ouabain binding to intact human erythrocytes. This ouabain displacing compound closely resembles ouabain in its polarity, molecular weight, non-peptidic nature and mode of action except for its UV absorbance spectrum. This compound sharing many biological activities of ouabain may be the endogenous ligand for the Na+, K+-ATPase and serve as a specific regulator of the sodium pump.
基于对[3H]-哇巴因与完整人红细胞结合的抑制作用，我们能够从人尿中纯化出一种洋地黄样因子，使其达到表观均一性。这种哇巴因置换化合物在极性、分子量、非肽性质和作用方式上与哇巴因极为相似，只是其紫外吸收光谱有所不同。这种具有许多哇巴因生物活性的化合物可能是Na +，K + -ATP酶的内源性配体，并作为钠泵的特异性调节剂。
