Abstract
Characterization of purified double-stranded RNA-activated eIF-2 alpha kinase from rabbit reticulocytes.
Highlights
The dsRNA-dependent eIF-2a kinase is present in lysates in an inactive form
At all stages of purificationof precursor of the 68.5K component. (b)Treatment of the latent dsI, activation was dependent on dsRNA and ATP and phosphorylated 68.5K polypeptide with crude lysate was accompaniedby the dsRNA-dependentphosphorylation protein phosphatases produceas shift t o the 67K poly- of a polypeptide doublet of67,000 and 68,500 daltons, peptide. (c) Protease digestion of the two polypeptides whichwerepresumed to be molecular components of dsI
Been purified tonear homogeneity by affinity chroma- In this report, we examine the relationship of these two tography on an agarose-poly[1] poly(C) matrix, from polypeptides to dsI and describe the further purification of which latent dsI can be eluted with 2 M KC1 and 100p~ latent dsI by affinity chromatography on agarose-poly[1]
Summary
The dsRNA-dependent eIF-2a kinase is present in lysates in an inactive form (latent dsI). (b)Treatment of the latent dsI, activation was dependent on dsRNA and ATP and phosphorylated 68.5K polypeptide with crude lysate was accompaniedby the dsRNA-dependentphosphorylation protein phosphatases produceas shift t o the 67K poly- of a polypeptide doublet of67,000 and 68,500 daltons (lo), peptide.
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