대두(Glycine max)축에 존재하는 diamine oxidase (EC 1.4.3.6)를 $(NH_4)_2SO_4$ 침전법, DEAE-cellulose, phosphocellulose, hydroxyapatite, affinity chromatography 등을 이용하여 정제하였다. 정제된 효소의 분자량은 Sephadex G-200 gel filtration에 의해 145,000으로 판명되었다. 정제된 효소는 SDS-PAGE 상에서 단일 띠를 나타냈다. 효소활성에 대한 최적 pH는 7.5였다. Putrescine은 이 효소에 대해 가장 좋은 기질이었으며 spermidine과 spermine도 기질로 작용하였다. Putrescine, spermidine, spermine에 대한 효소의 Km 값은 각각 $5.3{ imes}10^{-6}M$, $2.8{ imes}10^{-5}M$, $6.5{ imes}10^{-5}$이었다.
Diamine oxidase (EC 1.4.3.6) present in extracts of axes of soybean (Glycine max) seedling has been purified to homogeneity using series of ammonium sulfate fractionation, DEAE-cellulose, phosphocellulose, hydroxyapatite and 1,12-diaminododecane agarose column chromatography. The molecular weight estimated by a Sephadex G-200 gel filtration was about 145,000. Sodium dodecyl sulfate polyacrylamide gel electrophoresis gave a single band at the molecular weight of 70,000. The optimum pH for activity was 7.5. Putrescine was the best substrate, and spermidine and spermine also served as substrates in decreasing order. The $K_m$ values for putrescine, spermidine and spermine were $5.3{ imes}10^{-4}M$, $2.8{ imes}10^{-5}M$ and $6.5{ imes}10^5M$, respectively.
