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) |
|---|---|
| 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 |
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ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Association of a GDP binding activity with initiation factor eIF-2 from calf liver. / Stringer, Evan A.; Chaudhuri, Asok; Maitra, Umadas.
In: Biochemical and Biophysical Research Communications, Vol. 76, No. 2, 23.05.1977, p. 586-592.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Association of a GDP binding activity with initiation factor eIF-2 from calf liver
AU - Stringer, Evan A.
AU - Chaudhuri, Asok
AU - Maitra, Umadas
PY - 1977/5/23
Y1 - 1977/5/23
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0017393018&partnerID=8YFLogxK
U2 - 10.1016/0006-291X(77)90764-1
DO - 10.1016/0006-291X(77)90764-1
M3 - Article
C2 - 1036137
AN - SCOPUS:0017393018
VL - 76
SP - 586
EP - 592
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -