Purification and properties of rabbit reticulocyte protein synthesis elongation factor 2.
A homogeneous preparation of elongation factor 2 (EF-2) has been obtained from rabbit reticulocytes. EF-2, purified 1,960-fold, appears to be active as a single polypeptide chain with a molecular weight of approximately 100,000 based upon the following determinations: sodium dodecyl sulfate gel electrophoresis (95,000); sedimentation equilibrium centrifugation (112,000); gel filtration (97,000); ADP-ribosylation (103,000). The amino acid composition of rabbit reticulocyte EF-2 is almost identical with that of rat liver EF-2. The unknown amino acid in rat liver EF-2 which can be ADP-ribosylated appears also to be present in rabbit reticulocyte EF-2. A comparison of the amino acid composition of rabbit reticulocyte and rat liver EF-2 with Escherichia coli EF-G shows a high degree of similarity with only four amino acids differing by more than 10% (alanine, lysine, cysteine, and leucine).
D000241:Adenosine; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002845:Chromatography; D002848:Chromatography, DEAE-Cellulose; D002852:Chromatography, Ion Exchange; D004926:Escherichia coli; D006882:Hydroxyapatites; D008970:Molecular Weight; D009702:Nucleoside Diphosphate Sugars / Q000378:metabolism; D010445:Peptide Elongation Factors / Q000302:isolation & purification; D011487:Protein Conformation; D011817:Rabbits; D051381:Rats; D012156:Reticulocytes / Q000032:analysis* / Q000378:metabolism; D012266:Ribose; D014461:Ultracentrifugation
D000596:Amino Acids; D006882:Hydroxyapatites; D009702:Nucleoside Diphosphate Sugars; D010445:Peptide Elongation Factors; D012266:Ribose; D000241:Adenosine