한국산 무우로부터 Far Migrating Anionic isoperoxidase A3 의 정제 및 성질 = Purification and Characterization of the Far Migrating Anionic Isoperoxidase A3 from Korean Radish Root

다국어 초록 (Multilingual Abstract)

A far migrating anionic isoperoxidase, named A₃, was isolated from Korean radish (Raphanus sativas L.) root. Purification of the enzyme was accomplished by CM-cellulose chromatography, DEAF-Sephacel chromatography and Sephadex G-75 gel filtration. The enzyme was a glycoprotein having molecular weight of approximately 50,000 as determined by SDS-PAGE and Sephadex G-150 gel filtration and the pI value was 3.0. The optimum pH of the enzyme was 6.0 for guaiacol and H₂O₂and the Km values for guaiacol and H₂O₂ were 8 mM and 1 mM, respectively. Substrate studies with natural phenolic compounds were performed and their Km values were determined. In comparison with other Korean radish isoperoxidases, A₃ had higher affinity for esculetin. A particular interest is that the enzyme showed as sigmoidal substrate saturation curve against scopoletin despite of its single Subunit structure.