Possibility of the transformation of eEF-2 (100 kDa) to eEF-2 (65 kDa) in the peptide elongation process in vitro.
Two active eEF-2 polypeptides of approximately 100 and 65 kDa were copurified from rat liver cells and separated. The fate of eEF-2 (100 kDa) during its binding to ribosomes and in the translocation step of the peptide elongation process was investigated. It was shown that eEF-2 (100 kDa) did not change its form during the process of binding to the ribosomes. In the postribosomal supernatant, obtained from the postincubation mixture of the elongation process, only eEF-2 (65 kDa) was found. These results suggest that the form of eEF-2 (100 kDa), when bound to the ribosome during the elongation process, is transformed to eEF-2 (65 kDa).
Medical Academy, Institute of Chemistry, Bialystok, Poland.
A
A
Gajko
K
K
Sredzińska
W
W
Galasiński
A
A
Gindzieński
D000818:Animals; D002247:Carbon Isotopes; D002474:Cell-Free System; D002848:Chromatography, DEAE-Cellulose; D004591:Electrophoresis, Polyacrylamide Gel; D007930:Leucine / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D008297:Male; D008970:Molecular Weight; D010441:Peptide Chain Elongation, Translational; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000302:isolation & purification / Q000378:metabolism*; D011132:Polyribosomes / Q000378:metabolism; D020033:Protein Isoforms / Q000302:isolation & purification / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar
D002247:Carbon Isotopes; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D020033:Protein Isoforms; D007930:Leucine