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The resistance of wool to digestion by enzymes is probably due to a unique structure, consisting of peptide chains joined by disulfide cross-links to form a three-dimensional polymeric network of extremely high molecular weight. This conclusion is substantiated by a study of a series of derived wool proteins similar in composition but expected to differ in molecular weight. The proteins were prepared by first "depolymerizing" wool by reducing its disulfide cross-links to sulfhydryl groups, then making a series of solutions of this protein of widely varying ccncentration, and finally rebuilding the disulfide cross-links by reoxidation. An investigation of the rates of digestion by pepsin of a series of such proteins showed that those preparations expected to be of low molecular weight were rapidly digested, whereas those expected to be of greatest molecular weight were almost as resistant to digestion as untreated wool.

Dependence of the indigestibility of wool protein upon its polymeric structure