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Regulation of Protein Synthesis in Reticulocyte Lysates: Immune Serum Inhibits Heme-Regulated Protein Kinase Activity and Differentiates Heme-Regulated Protein Kinase from Double-Stranded RNA-Induced Protein Kinase
Ray Petryshyn, Hans Trachsel and Irving M. London
Proceedings of the National Academy of Sciences of the United States of America
Vol. 76, No. 4 (Apr., 1979), pp. 1575-1579
Published by: National Academy of Sciences
Stable URL: http://www.jstor.org/stable/69554
Page Count: 5
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A specific immune serum to the heme-regulated inhibitor (HRI) has been prepared by immunizing chickens with highly purified reversible HRI prepared from rabbit reticulocyte lysates. Studies with this immune serum demonstrate that the behavior of purified reversible HRI is similar to that of the inhibitor activated in rabbit reticulocyte lysates: the immune serum (i) inhibits the phosphorylation of the small subunit (38,000 daltons) of the eukaryotic initiation factor eIF-2 by both crude and purified inhibitor preparations; (ii) prevents the concomitant inhibition of protein synthesis by both crude and purified inhibitor preparations; and (iii) prevents the autophosphorylation of the 95,000-dalton polypeptide in purified and crude HRI preparations. The protein kinase and inhibitory activities of crude and partially purified preparations of the double-stranded RNA-induced inhibitor of protein synthesis are not affected by the immune serum prepared to reversible HRI. These results indicate that the inhibitor induced by double-stranded RNA is antigenically distinct from the reversible HRI.
Proceedings of the National Academy of Sciences of the United States of America © 1979 National Academy of Sciences