Isolation and properties of the subunit form EF-1C of elongation factor 1 from Guerin epithelioma cells

• Published in: Acta biochimica polonica Vol. 40; no. 2; pp. 225 - 230
• Main Authors: Marcinkiewicz, C, Gałasiński, W
• Format: Journal Article
• Language: English
• Published: Poland 1993
• Subjects: Animals; Carcinoma - chemistry; Electrophoresis, Polyacrylamide Gel; Guanosine Diphosphate - metabolism; Guanosine Triphosphate - metabolism; Liver - chemistry; Liver - metabolism; Macromolecular Substances; Neoplasm Proteins - isolation & purification; Neoplasm Proteins - metabolism; Neoplasm Proteins - pharmacology; Neoplasms, Experimental - chemistry; Peptide Biosynthesis; Peptide Elongation Factor 1; Peptide Elongation Factors - isolation & purification; Peptide Elongation Factors - metabolism; Peptide Elongation Factors - pharmacology; Peptides; Rats; Ribosomes - drug effects; Ribosomes - metabolism; RNA, Transfer, Phe - metabolism; Stimulation, Chemical; Tumor Cells, Cultured
• ISSN: 0001-527X; 1734-154X
• DOI: 10.18388/abp.1993_4822

EF-1C is a component of the aggregate EF-1B, consisting of the subunit forms EF-1A.EF-1C; it was isolated by dissociation of this aggregate in the presence of GTP. The subunit form EF-1C stimulates binding of aminoacyl-tRNA to ribosomes, catalysed by EF-1A, similarly as EF-1 beta gamma which stimulates the activity of EF-1 in other eukaryotic cells. EF-1C in the presence of 6 M urea was separated into two polypeptides. Polypeptide of molecular mass 32,000 Da is responsible for regeneration of the EF-1A.GTP active complex. Thermal sensitivity of EF-1A was much higher than that of EF-1B, thus a protective role of EF-1C in the EF-1A.EF-1C complex is suggested.