Formation of three-dimensional structure in protein fragments. Reactivation of reduced hen egg lysozyme fragment 1-127.
Regeneration of enzymic activity from reduced hen egg lysozyme peptide 1-127 was effected with a glutathione oxidation-reduction buffer. The rate of regeneration was nearly as great for peptide 1-127 as for reduced lysozyme itself, and the yields were the same (greater than 80%). The regenerated fragment 1-127 was shown to be indistinguishable from fragment 1-127 before reduction by ion exchange chromatography, amino acid analysis, polyacrylamide gel electrophoresis, and disulfide analysis. These results show that the COOH-terminal dipeptide Arg-Leu is not essential for the acquisition of the native three-dimensional structure of lysozyme.
D000596:Amino Acids / Q000032:analysis; D002268:Carboxypeptidases; D004220:Disulfides / Q000032:analysis; D009113:Muramidase / Q000378:metabolism*; D010446:Peptide Fragments; D011487:Protein Conformation
D000596:Amino Acids; D004220:Disulfides; D010446:Peptide Fragments; D009113:Muramidase; D002268:Carboxypeptidases