Abstract
Mouse immune interferon (IFNγ) induced double-stranded RNA-independent protein kinase activity in the cytoplasmic fraction of mouse L cells as measured against a histone substrate. Chromatographic purification separated the activity into three distinct kinases of molecular weights of approximately 100K (kinase I), 70K (kinase II), and 70K (kinase III). Partially purified IFNγ was as effective as crude in inducing protein kinase activity. Induction was blocked by treatment of IFNγ with specific anti-IFNγ antibody or by treatment of the L cells with actinomycin D. Kinase II activity was different from that of kinases I and III in that it showed Ca-dependence in the absence of Mg 2+, was inhibited in activity by the SH binding agent N-ethylmaleimide, and could use the cellular enzymes RNase A and hexokinase as substrates. The described protein kinases could play an important role in mediation of IFNγ effects, particularly where phosphorylated enzyme substrates were shown to have altered activity.
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