Abstract
A highly purified preparation of the eucaryotic initiation factor eIF-2 from calf liver which forms a ternary complex with GTP and Met-tRNAfMet also exhibits a potent GDP binding activity. The factor preparation specifically forms a binary complex with GDP, other ribonucleoside diphosphates and GTP are inactive. Evidence is presented indicating that the GTP-dependent Met-tRNAfMet binding and binary complex formation with GDP are mediated by the same protein which has an apparent molecular weight of 67,000 as judged by glycerol density gradient centrifugation.
Original language | English (US) |
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Pages (from-to) | 586-592 |
Number of pages | 7 |
Journal | Biochemical and Biophysical Research Communications |
Volume | 76 |
Issue number | 2 |
DOIs | |
State | Published - May 23 1977 |
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology