
pmid: 8780732
Comparison of the amino acid sequences of two peptides derived from proteolysis of rat liver pp49 identified it as composed of the beta-subunit and the gamma-subunit of eukaryotic initiation factor-2 (eIF-2). Partial purification of rat liver eIF-2 showed that its trimeric form (alpha beta gamma) co-eluted with protein kinase CK2. Heat-inactivated preparations of the trimeric form of eIF-2 inhibited CK2, increasing its Km for beta-casein, as observed with pp49. The form of eIF-2 that lacks the beta-subunit had no effect on CK2. These data indicate that the beta gamma subunits of eIF-2 may complex with CK2 and modulate its activity.
Sequence Homology, Amino Acid, Macromolecular Substances, Protein Conformation, Eukaryotic Initiation Factor-2, Molecular Sequence Data, Caseins, Proteins, In Vitro Techniques, Protein Serine-Threonine Kinases, Peptide Fragments, Rats, Liver, Animals, Humans, Amino Acid Sequence, Phosphorylation, Casein Kinase II
Sequence Homology, Amino Acid, Macromolecular Substances, Protein Conformation, Eukaryotic Initiation Factor-2, Molecular Sequence Data, Caseins, Proteins, In Vitro Techniques, Protein Serine-Threonine Kinases, Peptide Fragments, Rats, Liver, Animals, Humans, Amino Acid Sequence, Phosphorylation, Casein Kinase II
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