the disulphide bond in the wool at all until considerable degradation has occurred. Simple cystine polypeptides of varying compositions are now being synthesized to determine in which stereochemical arrangement if any the cystine disulphide bond cannot be oxidized by hypochlorite and permanganate. SUMMARY 1. A study has been made of the reaction of the disulphide bond in wool with different oxidizing agents. 2. Chlorine, hypochlorous acid and peracetic acid are capable of oxidizing all the cystine in wool, whereas acid permanganate and alkaline hypo-chlorite are only capable of oxidizing 25 % of the cystine present. The cystine in wool may therefore be divided into two fractions, one ofwhich is oxidized by the latter two reagents, and the other not. 3. The difference in reactivity of the two cystine fractions cannot be ascribed to morphological causes since the cystine of physically modified wools and powdered horn shows the same division. 4. The two fractions are not related to the Phillips (1946) cystine fractions. Possible explanations for the differences in reactivity are discussed. The authors wish to thank Messrs Wolsey Ltd., Leicester, for financial support which made this investigation possible, Prof. H. V. A. Briscoe for his help and interest, and Mr D. Gough for carrying out some of the preliminary experiments. * Previous papers in this series were published under the general title 'The Utilization of Urea in the Bovine Rumen'; see Smith & Baker (1944).