Abstract
SWAN1 has recently developed a method for solubilizing keratins which depends on the fission of cystine disulphide bonds by reaction with cupric and sulphite ions, with the formation of S-sulpho cysteine residues. The protein when modified in this way becomes water-soluble, with amino-acid residues other than cysteine and cystine unchanged. Swan's method has been applied by Pechère, Dixon, Maybury and Neurath2 to trypsinogen and chymotrypsinogen, and in these cases also the resulting S-sulpho derivatives were water-soluble.
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References
Swan, J. M., Nature, 180, 643 (1957).
Pechère, J. F., Dixon, G. H., Maybury, R. H., and Neurath, H., J. Biol. Chem., 233, 1364 (1958).
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McDERMOTT, E., PACE, J. Extraction of the Total Protein from Wheaten Flour in the Form of Soluble Derivatives. Nature 184, 546–547 (1959). https://doi.org/10.1038/184546b0
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DOI: https://doi.org/10.1038/184546b0
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