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brillar fragments in the homogenate of the muscle having the highest autolytic activity, it was shown that 160kD and 150kD proteins gradually appeared and myosin light chains disappeared during incubation at 15•Ž and pH 6.5. This degradation pattern was similar to that of muscles having the highest autolytic activity which were stored.

ECI, one of three isoforms of cysteine protease inhibitor found in chum salmon eggs was purified to homogeneity, and its complete amino acid sequence was determined. The primary structure of ECI did not resemble those of other cysteine protease inhibitors of the cystatin superfamily but did resemble that of a cysteine-rich motif found as a repetitive structural element in thyroglobulin and several other proteins. The function of the cysteine-rich motif is not yet hypothesis. Two cysteine motif proteins, thyroglobulin and entactin, were tested for papain inhibitory activity and found to have none.

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