Open AccessElongation Factor 1 from Krebs II Mouse Ascites Cells
Author(s) -
Drews Jürgen,
Bednarik Karl,
Grasmuk Hans
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03263.x
Subject(s) - sodium , ascites , elongation , enzyme , stoichiometry , elongation factor , molecular mass , biochemistry , eukaryotic translation elongation factor 1 alpha 1 , chemistry , ribosome , organic chemistry , medicine , rna , materials science , gene , metallurgy , ultimate tensile strength
A procedure for the purification of elongation factor 1 (EF‐1) from Krebs II mouse ascites cells is described. Ascites EF‐1 occurs in multiple forms of different molecular weight like the corresponding enzymes from calf brain and rat liver. Biogel A‐5m chromatography of our purest EF‐1 resulted in a pattern indicating the presence of different molecular weight components. However, only a single polypeptide band was observed when this same material was analysed by electrophoresis on acrylamide gels containing sodium dodecylsulphate. With this method the molecular weight of the EF‐1 polypeptide chain was determined to be 47000. It is suggested that the occurrence of multiple forms of EF‐1 is due to the association of 47000‐mol. wt subunits to form aggregates of different sizes. The factor has essentially the same enzymatic properties which were described for EF‐1 from reticulocytes, calf brain and rat liver. The attachment of aminoacyl‐tRNA to ribosomes catalyzed by EF‐1 follows a strict 1:1 stoichiometry. EF‐2 when introduced into the ribosomal binding assay allows the recycling of EF‐1 and subsequent synthesis of polypeptide chains. The possible implications of this finding with respect to the conditions which allow stoichiometric or catalytic function of EF‐1 are discussed.