This chapter reviews phosphorylation reactions that influence the activity of eIF-2. Important sites for translational control in eukaryotic systems appear to be reactions involving peptide initiation factor 2 (eIF-2). Phosphorylation is measured routinely by analysis of the reaction mixture on polyacrylamide gels in sodium dodecyl sulfate followed by autoradiography. Regulation of eIF-2 phosphorylation by phosphoprotein phosphatases may be an important control element. The relatively nonspecific phosphatase activities isolated thus far from reticulocytes may themselves be controlled by low-molecular-weight, heat-stable activators and inhibitors. Activators have been isolated that seem to impose a certain degree of substrate specificity on the reticulocyte phosphatase. © 1981, ACADEMIC PRESS, INC.
Kramer, G., & Hardesty, B. (1981). Phosphorylation Reactions That Influence the Activity of eIF-2. Current Topics in Cellular Regulation, 20(C), 185–203. https://doi.org/10.1016/B978-0-12-152820-1.50009-2