Walter R D
Hoppe Seylers Z Physiol Chem. 1978 May;359(5):607-12. doi: 10.1515/bchm.1978.359.1.607.
Two cyclic AMP-binding proteins, not identical with regulatory subunits of protein kinases, have been isolated from Trypanosoma gambiense. The cyclic AMP receptors were separated by gel chromatography on the basis of their molecular weights. The binding constants of the high and the low molecular weight receptors for cyclic AMP were determined to be 0.4 muM and 0.6 muM, respectively. Cyclic IMP and cyclic GMP compete with cyclic AMP for the binding sites of both receptors. The cyclic AMP binding of the low molecular weight receptor was competitively inhibitied by adenine derivatives. The binding capacity of the high molecular weight receptor was enhanced about two-fold by proteolytic modification with trypsin.
从冈比亚锥虫中分离出了两种环磷酸腺苷结合蛋白，它们与蛋白激酶的调节亚基不同。环磷酸腺苷受体通过凝胶色谱法根据其分子量进行分离。已确定高分子量和低分子量受体对环磷酸腺苷的结合常数分别为0.4微摩尔和0.6微摩尔。环磷酸肌苷和环磷酸鸟苷与环磷酸腺苷竞争两种受体的结合位点。低分子量受体的环磷酸腺苷结合被腺嘌呤衍生物竞争性抑制。用胰蛋白酶进行蛋白水解修饰后，高分子量受体的结合能力增强了约两倍。
