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- W2156804512 abstract "Formation of native lysozyme from the reduced form involves many pathways in two processes: incorrect pairing of half-cystine residues by oxidation and rearrangement of disulfide (SS) bonds. The energy barrier against suflhydryl (SH)-disulfide interchange of the native or nativelike species thus formed causes accumulation of these species. For example, the enzymatically active isomers containing three presumably native SS bonds and one open SS bond may be thermodynamically favorable over the nonnative isomers and can be formed from reduced lysozyme or lysozyme containing scrambled SS bonds by nonobligatory and flexible pathways. As an extension of these observations formation of nativelike species from reduced lysozyme containing the average of two carboxymethyl (CM)-cysteine was investigated." @default.
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- W2156804512 date "1980-10-01" @default.
- W2156804512 modified "2023-09-30" @default.
- W2156804512 title "On the renaturation of reduced hen egg white lysozyme containing two blocked sulfhydryl groups" @default.
- W2156804512 cites W1997263964 @default.
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- W2156804512 doi "https://doi.org/10.1016/s0006-3495(80)84967-8" @default.
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