Double-stranded RNA dependent protein kinase (s) in rabbit reticulocyte lysates analogous to kinase from interferon-treated cells.

A double-stranded (ds) RNA-dependent protein kinase(s) from haemin-supplemented rabbit reticulocyte lysates in purified by chromatography on columns of poly(I).poly(C)-Sepharose. This method provides a more than 1000-fold purifications of the kinase(s) in a single step and a high yield. The purified kinase is responsible for the phosphorylation of (a) a polypeptide of molecular weight 67000, (b) the smallest subunit eIF-2 and (c) added histones. These kinase activities are comparable to the dsRNA-dependent protein kinase activities from interferon-treated cells.