Isolation and properties of elongation factor 1 from Saccharomyces cerevisiae

Acta Microbiol Pol. 1981;30(2):111-21.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Fungal Proteins / analysis
  • Fungal Proteins / isolation & purification*
  • Isoelectric Point
  • Molecular Weight
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors / analysis
  • Peptide Elongation Factors / isolation & purification*
  • Peptides / analysis
  • Saccharomyces cerevisiae / analysis*

Substances

  • Fungal Proteins
  • Peptide Elongation Factor 1
  • Peptide Elongation Factors
  • Peptides