Galabru J, Hovanessian A G
Cell. 1985 Dec;43(3 Pt 2):685-94. doi: 10.1016/0092-8674(85)90241-7.
The double-stranded (ds) RNA-dependent protein kinase is a 100,000-110,000 Mr complex of two interferon-induced subunits each having ATP binding sites: a 48,000 Mr protein (p48) which appears to be responsible for the phosphorylation of a 68,000 Mr protein (p68) in the presence of dsRNA. The p68 subunit once phosphorylated is converted to an active protein kinase capable of phosphorylating exogenous substrates such as the alpha subunit of protein synthesis initiation factor eIF2 or calf thymus histone. The phosphorylation of exogenous substrates is highly correlated with the degree of phosphate saturation of p68 and does not require the presence of dsRNA. Both the p68 and the p48 subunits of the protein kinase complex are purified by an immuno-affinity column containing monoclonal antibody specific for the p68 subunit.
双链（ds）RNA依赖性蛋白激酶是一种分子量为100,000 - 110,000的复合物，由两个干扰素诱导的亚基组成，每个亚基都有ATP结合位点：一个48,000分子量的蛋白质（p48），在双链RNA存在的情况下，它似乎负责对一个68,000分子量的蛋白质（p68）进行磷酸化。p68亚基一旦被磷酸化，就会转化为一种活性蛋白激酶，能够对外源底物进行磷酸化，如蛋白质合成起始因子eIF2的α亚基或小牛胸腺组蛋白。外源底物的磷酸化与p68的磷酸饱和程度高度相关，并且不需要双链RNA的存在。蛋白激酶复合物的p68和p48亚基都通过含有针对p68亚基的单克隆抗体的免疫亲和柱进行纯化。
