Milk-clotting enzyme from microorganisms. XII. Physicochemical and immunochemical studies on similarities of acid proteases Mucor pusillus rennin and Mucor miehei rennin.

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Abstract
Physicochemical and immunochemical comparisons were made on the two acid proteases Mucor pusillus rennin (MPR) and Mucor miehei rennin (MMR). The molecular weight and isoelectric points of the two enzymes were similar: MPR (M. W., 38, 500 and I. P., 3.9) vs. MMR (M. W., 42, 000 and I. P., 4.1). D-Galactose and D-glucosamine, which had been found in MMR, were also detected in the carbohydrate moiety of MPR with gas-chromatography and amino acid analyses. The structural similarity between MPR and MMR was investigated utilizing peptide mapping techniques, which showed a close correlation between the two enzymes. Furthermore, immunodiffusion test using antisera prepared against each enzyme suggested the presence of a common antigenic structure. The results confirm, that a high similarity exists between MPR and MMR, which has been supposed from the morphological identity of the two enzyme-producing fungal strains.

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