Azhaeva E V, Severin S E, Kondrat'ev A D
Biokhimiia. 1987 Nov;52(11):1781-5.
The kinetic properties of cyclic nucleotide phosphodiesterase isolated from the cytoplasmic fraction of lymphoblastoma QOS cells were studied. It was demonstrated that the enzyme can be activated in the presence of micromolar concentrations of cGMP. The kinetic properties of the enzyme are characterized by the nonlinear dependence of the cAMP hydrolysis rate on the substrate concentration. The curve becomes linear in the presence of cGMP. The molecular mass of phosphodiesterase as determined from gel filtration data is 80,0000 Da.
对从淋巴瘤QOS细胞胞质部分分离出的环核苷酸磷酸二酯酶的动力学特性进行了研究。结果表明,该酶在微摩尔浓度的环鸟苷酸(cGMP)存在下可被激活。该酶的动力学特性表现为环磷酸腺苷(cAMP)水解速率对底物浓度呈非线性依赖。在环鸟苷酸存在时,曲线变为线性。根据凝胶过滤数据测定的磷酸二酯酶分子量为80,000 Da。