Haeffner E W, Holl A
Int J Biochem. 1984;16(12):1245-50. doi: 10.1016/0020-711x(84)90223-4.
The glycogen-containing ascites cell line was found to have a 3-5 times higher 5'-nucleotidase specific activity than the glycogen-free variant, resulting in different substrate affinity constants of Km = 0.14 mM and Km = 0.69 mM respectively. These activity differences were due to true 5'-nucleotidase as shown by its inactivation through specific inhibitors such as concanavalin A and alpha, beta-methylene adenosine diphosphate. Substrate specificity of the enzyme was similar in both cell lines, but differences were observed with respect to the pH optimum and stability.
发现含糖原的腹水细胞系的5'-核苷酸酶比活性比无糖原变体高3至5倍，导致底物亲和常数分别为Km = 0.14 mM和Km = 0.69 mM。这些活性差异是由于真正的5'-核苷酸酶，如伴刀豆球蛋白A和α,β-亚甲基二磷酸腺苷等特异性抑制剂使其失活所显示的那样。两种细胞系中该酶的底物特异性相似，但在最适pH和稳定性方面存在差异。
