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Disulfide content of reduced hen egg white and human milk lysozymes during the folding process
Author(s) -
Perraudin Jean-Paul,
Guillard Roger,
Prieels Jean-Paul,
Torchia Timothy,
Thierry Dubois
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80640-1
Subject(s) - lysozyme , disulfide bond , egg white , chemistry , folding (dsp implementation) , muramidase , kinetics , protein folding , biochemistry , food science , physics , quantum mechanics , electrical engineering , engineering
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.