Ilson D H, Torrence P F, Vilcek J
J Interferon Res. 1986 Feb;6(1):5-12. doi: 10.1089/jir.1986.6.5.
Ion-exchange and gel filtration chromatography were used to purify partially a 33,000-dalton (33 kD) 2',5'-oligoadenylate synthetase and a 110,000-dalton (110 kD) 2',5'-oligoadenylate synthetase from HeLa cells treated with alpha-interferon (IFN-alpha). The 33-kD enzyme was optimally activated only when double-stranded RNA was added in 100 to 1000-fold excess of the concentration activating the 110-kD enzyme. Certain double- or triple-stranded RNAs, which were observed to activate the 110-kD enzyme, failed to activate the 33-kD enzyme, even when added at high concentration. The 110-kD enzyme manifested an alkaline pH optimum of 7.5 or more and the 33-kD enzyme an acidic pH optimum of 6.0 or less. The results suggest that intracellular activation of the two forms of 2',5'-oligoadenylate synthetase may occur under markedly different conditions.
采用离子交换和凝胶过滤色谱法，从经α-干扰素（IFN-α）处理的HeLa细胞中部分纯化出一种33000道尔顿（33 kD）的2',5'-寡腺苷酸合成酶和一种110000道尔顿（110 kD）的2',5'-寡腺苷酸合成酶。只有当双链RNA的添加量比激活110 kD酶的浓度高100至1000倍时，33 kD酶才能被最佳激活。某些能激活110 kD酶的双链或三链RNA，即使高浓度添加也无法激活33 kD酶。110 kD酶的最适碱性pH值为7.5或更高，33 kD酶的最适酸性pH值为6.0或更低。结果表明，两种形式的2',5'-寡腺苷酸合成酶在细胞内的激活可能发生在明显不同的条件下。
