Abstract
INVESTIGATIONS of acid hydrolysates of wool labelled with sulphur-35, and of non-radioactive wool hydrolysed with 35S-cystine, have shown the presence of unidentified sulphur compounds derived from cystine1,2. The most abundant of these (I) increased in amount with increasing time of hydrolysis up to 100 hr., when about one-tenth of the original sulphur in wool was present as (I). Somewhat smaller amounts of (I), representing about one-fiftieth of the protein sulphur, were found in acid hydrolysates of insulin, ribonuclease and bovine serum albumin, but none could be detected in hydrolysates of lysozyme and β-lactoglobulin.
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FLETCHER, J., ROBSON, A. Occurrence of Bis(β-Amino-β-Carboxy-ethyl) Trisulphide in the Hydrolysates of Wool and other Proteins. Nature 195, 1308 (1962). https://doi.org/10.1038/1951308a0
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DOI: https://doi.org/10.1038/1951308a0
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