Abstract
Eukaryotic protein synthesis initiation factor 2 (eIF-2), a heterotrimer, was chromatographed on high performance (Superose 6) and standard (Ultrogel AcA 34 and Sephacryl S-300) size exclusion chromatography (SEC) media. The retention volume of eIF-2 on the Superose 6 column was higher than expected from its Mr and elution of a βγ eIF-2 dimer was seen. Conversely, on AcA 34 and Sephacryl S-300 most of the eIF-2 was eluted at its expected position, considering its ellipsoidal structure, as the heterotrimer. Elution of the βγ heterodimeric eIF-2 may therefore be promoted by Superose 6 high performance SEC which therefore provides a means for its rapid preparation for studies in protein synthesis initiation.
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