Purification and enzymatic peptide mapping of protein synthesis elongation factor-2 from mink and chicken livers.
This investigation has shown it it possible to purify elongation factor-2 from livers of two rather distinct animal species, minks and chicken, to high homogeneity by employing the same purification procedure. It is also shown that making peptide maps of the factor by the use of Staphylococcus aureus Endoprotease Glu-C gives the same pattern. Combined, these two experimental approaches show that the evolution has conserved this elongation factor in two species with a rather different physiology and choice of feeding substances. It is also shown that using mink or chicken livers as staring material for purification of eEF-2 is both technically and economically sound when obtaining large amounts of highly purified eEF-2 is the ultimate goal.
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Department of Product Quality, Danish Institute of Animal Science, Research Centre Foulum, Tjele, Denmark.
D000818:Animals; D002645:Chickens; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008099:Liver / Q000737:chemistry*; D008907:Mink; D009419:Nerve Tissue Proteins / Q000737:chemistry / Q000302:isolation & purification*; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000302:isolation & purification*; D010449:Peptide Mapping; D010750:Phosphoproteins / Q000737:chemistry / Q000302:isolation & purification*; D011487:Protein Conformation
D009419:Nerve Tissue Proteins; D020652:Peptide Elongation Factor 2; D010445:Peptide Elongation Factors; D010750:Phosphoproteins