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 |
Fingerprint
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.
UR - http://www.scopus.com/inward/record.url?scp=0017393018&partnerID=8YFLogxK
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 -