TY - JOUR
T1 - Protein synthesis in rabbit reticulocytes XIX
T2 - EIF-2 promotes dissociation of Met-tRNAf·EIF-1·GTP complex and Met-tRNAf binding to 40S ribosomes
AU - Majumdar, A.
AU - Roy, R.
AU - Das, A.
AU - Dasgupta, A.
AU - Gupta, N. K.
N1 - Funding Information:
Acknowledgements research work was supported by NIH Research Grants GM-18796 The authors thank Mr. Dennis Jurgens for the preparation ribosomes and ribosomal salt wash.
PY - 1977/9/9
Y1 - 1977/9/9
N2 - The peptide chain initiation factor, EIF-2 has been partially purified from the 0.5 M KCl ribosomal wash. The molecular weight of EIF-2 is approximately 450,000. The purified EIF-2 preparation promotes the dissociation of the ternary complex, Met-tRNAf·EIF-1·GTP in the presence of Mg++ and is also required along with EIF-1 for AUG-directed Met-tRNAf binding to 40S ribosomes.
AB - The peptide chain initiation factor, EIF-2 has been partially purified from the 0.5 M KCl ribosomal wash. The molecular weight of EIF-2 is approximately 450,000. The purified EIF-2 preparation promotes the dissociation of the ternary complex, Met-tRNAf·EIF-1·GTP in the presence of Mg++ and is also required along with EIF-1 for AUG-directed Met-tRNAf binding to 40S ribosomes.
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U2 - 10.1016/0006-291X(77)91235-9
DO - 10.1016/0006-291X(77)91235-9
M3 - Article
C2 - 907668
AN - SCOPUS:0017753214
VL - 78
SP - 161
EP - 169
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -