Proteins contained in the effusions of serous otitis media were analyzed by Disc electrophoresis. The electrophoretic patterns were compaired with those of serum from the same patients.
The number of protein fractions was less than that of serum from the same patient. The most distinct characteristics of the electrophoretic patterns of the effusions was that S_β fraction disappeared, haptoglobins became indistinct and gamma globulin increased in all cases.

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Alkaline phosphatase isozyme of serum and tissue extracts were studied by electrophoresis using polyacrylamide as a supporting medium. Location of the enzyme activity were determined by diazo-coupling staining method.
Four separate zones of the enzyme activity were found in various tissue extracts of normal rabbit and human origin, and in normal and pathological human sera.
Sera from patients with liver or bone disease showed specific patterns of alkaline phosphatase activity.
Sera from patients with obstruction of hepatic or common biliary duct and the bone extracts of the same patient showed analogous isozyme patterns.

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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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The authors have been using immunochemical techniques for studying the structure and biosynthesis of rat catalase, and the present paper reports the results of a few investigations on the precipitin reaction between catalase and anti-catalase: specificity of the reaction, and quantitative assay method for determining the catalase antigen, separation of catalase from its complex with antibody etc.

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