Disulfide content of reduced hen egg white and human milk lysozymes during the folding process |
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| Authors: | J P Perraudin R Guillard J P Prieels T Torchia T Dubois |
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| Institution: | 1. Department of Medicine, University of Western Ontario, London, Canada;2. Department of Chemistry I, Karolinska Institutet, Stockholm, Sweden;3. Department of Biochemistry II, Karolinska Institutet, Stockholm, Sweden |
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| Abstract: | In order to obtain a better understanding of the possible influence of the primary sequence of a protein on its folding pathway, renaturation of reduced human milk lysozyme was compared to that of reduced hen egg white lysozyme. Following disulfide bond formation, under identical conditions, similar products were found during the folding of both lysozymes, but the kinetics of appearance and disappearance of these intermediates as well as the appearance of the native conformation were different. |
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| Keywords: | Gastrin-releasing peptide (GRP) Bombesin Gastrin release HPLC Ion-exchange chromatography β-Aspartyl shift |
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