Abstract
A factor has been isolated from wheat germ that enhances the ability of initiation factor 2 (eIF-2) to form a ternary complex with GTP and Met-tRNAf and enhances the binding of Met-tRNAf to 40 s ribosomal subunits. This factor, designated Co-eIF2 beta, is a monomeric protein with a molecular weight of approximately 83,000. Wheat germ eIF-2 forms a stable binary complex with GDP but not with GTP. Co-eIF-2 beta enhances the formation of an eIF-2 . GDP complex, but does not enable eIF-2 to form a stable complex with GTP.
Highlights
From the DeDartment of Chemistrv and Clayton Foundation Biochemical Institute, The University of Texas at Austin, Austin, Teras 78712 ’
Purification of Co-eZF-2a”The 40 to 60% ammonium sulfate fraction of the 120 mM KC1 postribosomal supernatant derived from 400 g of wheat germ was prepared (17, 18) and chromatographed on DEAE-cellulose as previously described (15)
The column was developed with sulfate fractionof the 120 mM KC1postribosomal supernatant Buffer B-100, and 1.5-ml fractions were collected at a flow rate of 9 from wheat germ that enhanced the activity of enhance the abilityof initiation factor 2 (eIF-2)
Summary
From the DeDartment of Chemistrv and Clayton Foundation Biochemical Institute, The University of Texas at Austin, Austin, Teras 78712 ’. The Co-eIF-2a activity eluted between 250 forma ternary complex with Met-tRNAf and GTP and to and 300 mM KC].
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