Purification and properties of the heterogeneous subunits of elongation factor EF-1 from Guerin epithelioma cells.
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.
Marcinkiewicz
C
C
Department of General and Organic Chemistry, Medical Academy, Białystok, Poland.
Gajko
A
A
Gałasiński
W
W
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
D009363:Neoplasm Proteins; D020648:Peptide Elongation Factor 1; D010445:Peptide Elongation Factors; D012346:RNA, Transfer, Amino Acyl; D012261:Ribonucleoproteins