Isolation and properties of elongation factor 1 from Saccharomyces cerevisiae.
Polypeptide elongation factor 1 was isolated from yeast postribosomal supernatant. The highly purified factor was resolved on Ultrogel AcA-44 into two complementary fractions. One of these fractions contained two different polypeptide chains corresponding to a Ts-like elongation factor EF-1 beta gamma. The other fraction represented the light form of the factor, designated EF-1 alpha, with a molecular weight of approximately 50,000. The obtained results indicate that EF-1 from lower eukaryotes is also composed of three distinct polypeptides.
D005656:Fungal Proteins / Q000032:analysis / Q000302:isolation & purification*; D007526:Isoelectric Point; D008970:Molecular Weight; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000032:analysis / Q000302:isolation & purification*; D010455:Peptides / Q000032:analysis; D012441:Saccharomyces cerevisiae / Q000032:analysis*
D005656:Fungal Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D010455:Peptides