Abstract
Initiation factor 2 from adult rat brain was isolated from salt-washed microsomes using a three-step purification process consisting of heparin-Sepharose, phosphocellulose and diethylaminoethyl-cellulose (DEAE-cellulose) column chromatographics. The initiation factor 2 (eIF-2) was phosphorylated in subunits α and β by the endogenous protein kinase activity present in the purified preparation. This protein kinase activity proved to be mostly a casein kinase, although the possible presence of a very specific α kinase activity cannot be dismissed.
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