The elongation factor 1 from wheat germ: structural and functional properties.
Three forms of elongation factor 1 (EF1A, EF1B and EF1C) were isolated from wheat germ; the preparation obtained by successive chromatography on DEAE-Sephadex A-50, hydroxylapatite and Sephadex G-200 showed about 90% purity. The molecular masses of these forms were about: 61 000, 48 000 and 12 500, respectively. EF1A was the only form which formed the ternary complex GTP-EF1-AA-tRNA and was the most active in binding of Phe-tRNA to the poly-U programmed ribosomes. Based on the data of amino acid analysis, N-terminal amino acid determination and previously described proteolysis (Pulikowska et al., Biochem. Biophys. Res. Commun., 1979, 91, 1011-1017), it is assumed that EF1C is a basic structural subunit of elongation factor EF1 from wheat germ, but only EF1A shows the conformation-dependent full biological activity.
D000596:Amino Acids / Q000032:analysis; D055598:Chemical Phenomena; D002621:Chemistry; D003931:Diacetyl / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D005672:Fusidic Acid / Q000494:pharmacology; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000032:analysis* / Q000378:metabolism; D010455:Peptides / Q000032:analysis; D011485:Protein Binding; D013033:Sparsomycin / Q000494:pharmacology; D014908:Triticum / Q000032:analysis*
D000596:Amino Acids; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010455:Peptides; D005672:Fusidic Acid; D013033:Sparsomycin; D003931:Diacetyl