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Some properties of amine oxidase from soybean seedlings.

The purpose of the present study was to clarify the properties of amine oxidase partially purified from soybean seedlings, which the authors used as an enzyme sample for the assay of diamines (putrescine, cadaverine) and polyamines (spermidine, spermine). The enzyme activity was highest with cadaverine followed by putrescine, spermidine, L7-diaminoheptane and spermine. The optimum pH was 7.8 for putrescine and cadaverine and 8.0 for spermidine and spermine. Carbonyl reagents, such as semicarbazide, and chelating reagents, such as cuprizone, were effective inhibitots of soybean seedling amine oxidase (SSAO), suggesting that Cu" and pyridoxal may be cofactors for SSAO. Therefore, SSAO appeared to be a diamine oxidase (EC 1.4.3.6). It was stable at 50°C for at least 2 hours, and the apparent K", values for all diamines and polyamines were extremely low. Since SSAO is present in great quantities in soybean seedlings, which can be easily obtained in every season in Japan, it is very suitable asan enzyme sample for the assay of diamines and polyamines.