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1 factor 2 (IF-2) and eukaryotic IF-2 (eIF-2)/eIF-2B, i.e., the initiation factors involved in introdu
2 -subunit of eukaryotic initiation factor 2B (eIF-2B), a guanine nucleotide exchange protein that func
5 binant eIF-2B had the same molecular mass as eIF-2B purified from rat liver and that it did indeed po
7 on of the guanine nucleotide exchange factor eIF-2B, without altering the apparent dissociation const
8 n of the guanine nucleotide exchange factor (eIF-2B) by casein kinase 2 (CK-2) was previously shown t
10 the guanine nucleotide exchange activity of eIF-2B in heme-deficient RRL and in hemin-supplemented R
11 s approximately 0.27 mol of phosphate/mol of eIF-2B and doubles guanine nucleotide exchange activity.
12 is much less (approximately 0.12 mol/mol of eIF-2B in both preparations) than that obtained with CK-
13 tion with CK-1 (0.49 mol of phosphate/mol of eIF-2B) restores its specific activity to that of the ph
14 this study indicate that phosphorylation of eIF-2B with CK-1 and/or CK-2 is required for GTP binding
16 o presented for a mechanism of regulation of eIF-2B activity whereby phosphorylation by GSK-3 influen
18 tro phosphorylation of the 82-kDa subunit of eIF-2B by CK-1 and glycogen synthase kinase 3 (GSK-3) an
21 ion chromatography revealed that recombinant eIF-2B had the same molecular mass as eIF-2B purified fr
22 of the gene family defined by the (related) eIF-2B subunits alpha, beta, and delta, although these a
23 hibited the GEF activity of the five-subunit eIF-2B; this inhibition required the eIF-2B alpha-subuni
26 th isolated and alkaline phosphatase-treated eIF-2B; however, the stoichiometry of phosphorylation is
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