Multiformity of elongation factor eEF-2 isolated from rat liver cells.
Two fractions of eEF-2 (M(r) approx. 100,000 and M(r) approx. 65,000) were isolated from post-ribosomal supernatant of the rat liver cells. Only eEF-2, with mol. weight of about 100,000 Da, can be phosphorylated, but only eEF-2, with mol. weight of about 65,000 Da, was isolated from the active polyribosomes. The existence of two eEF-2 forms with different properties in the rat liver cells is striking and uncovers new aspects for the cellular function of this protein.
Gajko
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Department of General and Organic Chemistry, Institute of Chemistry, Medical Academy, Białystok, Poland.
Gałasiński
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Gindzieński
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D000645:Ammonium Sulfate; D000818:Animals; D002118:Calcium / Q000494:pharmacology; D002147:Calmodulin / Q000378:metabolism; D002499:Centrifugation, Density Gradient; D011232:Chemical Precipitation; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008099:Liver / Q000737:chemistry*; D008297:Male; D008970:Molecular Weight; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000302:isolation & purification* / Q000378:metabolism; D010766:Phosphorylation; D011132:Polyribosomes / Q000737:chemistry; D011494:Protein Kinases / Q000378:metabolism; D051381:Rats; D017208:Rats, Wistar
D002147:Calmodulin; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D011494:Protein Kinases; D000645:Ammonium Sulfate; D002118:Calcium