Article
Evidence for difference in the roles of two cysteine residues involved in disulfide bond formation in the folding of human lysozyme.
The Journal of biological chemistry - 5 May 1990
Taniyama Y, Yamamoto Y, Kuroki R, Kikuchi M
Abstract excerpt
Human lysozyme is made up of 130 amino acid residues and has four disulfide bonds at Cys6-Cys128, Cys30-Cys116, Cys65-Cys81, and Cys77-Cys95. Our previous results using the Saccharomyces cerevisiae secretion system indicate that the individual disulfide bonds of human lysozyme have different functions in the correct in vivo folding and enzymatic activity of the protein (Taniyama, Y., Yamamoto, Y., Nakao, M.,...
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