title: Purification and properties of the heterogeneous subunits of elongation factor EF-1 from Guerin epithelioma cells.
abstract: Elongation factor EF-1 from Guerin epithelioma was separated into two subunit forms EF-1A and EF-1B by chromatography in the presence of 25% glycerol, successively on CM-Sephadex and DEAE-Sephadex. It was shown that EF-1A is a thermolabile, single polypeptide which catalyses the binding of aminoacyl-tRNA to ribosomes, similarly as eukaryotic EF-1 alpha or prokaryotic EF-Tu. EF-1B was characterized as a complex composed of at least two polypeptides. One of them is EF-1A, the other EF-1C, which stimulates EF-1A activity and protects this elongation factor from thermal inactivation.
authors.affiliation: Department of General and Organic Chemistry, Medical Academy, Białystok, Poland.
authors.forename: C
authors.initials: C
authors.lastname: Marcinkiewicz
authors.forename: A
authors.initials: A
authors.lastname: Gajko
authors.forename: W
authors.initials: W
authors.lastname: Gałasiński
mesh_terms: D000818:Animals; D002277:Carcinoma / Q000737:chemistry* / Q000473:pathology; D002850:Chromatography, Gel; D009363:Neoplasm Proteins / Q000737:chemistry / Q000302:isolation & purification*; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000302:isolation & purification*; D011487:Protein Conformation; D012346:RNA, Transfer, Amino Acyl / Q000378:metabolism; D051381:Rats; D012261:Ribonucleoproteins / Q000737:chemistry / Q000302:isolation & purification; D014407:Tumor Cells, Cultured
chemical_list: D009363:Neoplasm Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D012261:Ribonucleoproteins