The action of trypsin on oxidized normal and copper-deficient wool has been ex amined by ( i ) N -terminal-residue estimations and (ii) paper electrophoresis and chromatography on the tryptic digests. Trypsin readily solubilizes oxidized wool but does not digest it completely, probably because of its high cysteic-acid concentration. Little difference was found between normal and copper-deficient wool, although the latter gave a smaller amount of a certain group of acidic peptides. Preliminary tests on the chromatography of the tryptic digests using ion-exchange resins are reported.
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