Multiple Forms of Elongation Factor 1 from Calf Brain
- 1 December 1973
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 70 (12) , 3282-3286
- https://doi.org/10.1073/pnas.70.12.3282
Abstract
Heavy and light forms of elongation factor 1 (EF-1) from calf brain have been partially purified. The heterogeneous heavy species (EF-1(H)) with molecular weights of 2.5 x 10(5) to over 1 x 10(6) appears to be a complex or aggregate of the light form of the enzyme (EF-1(L)); the latter has a molecular weight of between 50,000 and 60,000. EF-1(H) but not EF-1(L), contains significant amounts of free and esterified cholesterol. Although EF-1(H) and EF-1(L) are both active in aminoacyl-tRNA binding to ribosomes, EF-1(L) reacts with GTP and aminoacyl-tRNA more efficiently than EF-1(H).Keywords
This publication has 17 references indexed in Scilit:
- The role of cholesteryl 14-methylhexadecanoate in peptide elongation reactionsBiochemical Journal, 1971
- Fluorometric determination of cholesterol and cholesteryl ester in tissue on the nanogram levelAnalytical Biochemistry, 1971
- Further studies on the role of factors Ts and Tu in protein synthesisArchives of Biochemistry and Biophysics, 1971
- Studies on the role of factor Ts in aminoacyl-tRNA binding to ribosomesArchives of Biochemistry and Biophysics, 1970
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Interactions between the elongation factors: The displacement of GDP from the Tu-GDP complex by factor TsBiochemical and Biophysical Research Communications, 1970
- Studies on the role of factor Ts in polypeptide synthesisArchives of Biochemistry and Biophysics, 1970
- Purification and Partial Characterization of the Aminoacyl Transfer Ribonucleic Acid Binding Enzyme from Rabbit ReticulocytesJournal of Biological Chemistry, 1969
- Effect of lipids, in particular cholesteryl 14-methylhexadecanoate, on the incorporation of labelled amino acids into transfer ribonucleic acid in vitroBiochemical Journal, 1968
- The isolation and biological activity of multiple forms of aminoacyl transferase I of rat liverBiochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis, 1968