Beef liver catalase prepared by the method of Deutsch was further purified by DEAF-cellulose chromatography and Sephadex G-200 gel filtration.
Tyrosine to tryptophan ratio of the preparation was found to be 1.84 by the ultraviolet absorption spectrophotometric method devised by Bencz. Tyrosine content of the preparation was estimated to be 80 moles per mole by the same method, while, that obtained by ion-exchange chromatographic analysis of hydrochloric acid hydrolyzate of the preparation was 84 moles per mole.
Ultraviolet absorption of the preparation at 292mμ showed stepwise increase at pH 10.5 and 13 with the simultaneous increase in fluorescence. The increase around the latter pH was found to be several times greater than that at the former pH. The results indicate that most of the tyrosine molecules are folded into the inner portion of the catalase molecule.
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