풍부한 해양생물인 진주담치의 조직으로부터 분리정제된 superoxide dismutase(SOD)는 1%의 수율로 264배 정제되었다. 황산암모늄 처리, DEAE-Sephadex A-50 이온교환 크로마토그래피, Sephadex G-100 겔크로마토그래피를 이용해 정제된 효소는 Sephadex G-100 겔여과 방법으로 측정된 분자량이 105.4 kDa이었으며, SDS-polyacrylamide 전기이동을 행한 결과 52.9 kDa의 2개의 subunit로 구성된 homodimer 임이 밝혀졌다. 이 효소는 $25^{circ}C$에서 완충용액의 pH가 6에서 8.3사이일 때는 매우 안정하였지만 pH5.0 이하나 pH 10.5 이상에서는 활성이 급격히 저해되었고, $CN^-$, $Cl^-$, $H_{2}O_{2}$, EDTA, SDS 농도에 비례하여서 활성이 억제되었다. 그러나 $N_{3}^{-}$는 효소활성에 영향을 주지 못하였다. 그리고 520nm와 265nm에서 최대의 흡광을 나타내었으며, 265nm에서의 흡광은 cysteine에 의해 쉽게 환원되었다. 또한 원자흡광분석기에 의해 측정된 결과, 효소몰당 2atom씩의 $Cu^{2+}$, $Zn^{2+}$가 각각 포함되어 있어 진주담치로부터 분리된 이 효소가 Cu/Zn-SOD임을 확인하였다.
Superoxide dismutase (SOD) was isolated by direct extraction method from the muscular tissue of Mytilus edulis. The enzyme was purified 264-fold with 1 % yield for the cytosolic SOD by $(NH_{4})_{2}SO_{4}$ fractionation, DEAE-Sephadex A-50 ion exchange chromatography and Sephadex G-100 gel chromatography. The molecular weight of the enzyme estimated from gel filtration on Sephadex G-100 was approximately 105.4 kDa and SDS-polyacrylamide gel electrophoresis also showed that it was composed of two identical subunits whose molecular weight was 52.9 kDa. The purified enzyme stably remained between pH 6 and pH 8.3 at $25^{circ}C$, but was rapidly inactivated above pH 10.5 and below pH 5.0. This enzyme was easily inhibited by $CN^-$, $Cl^-$, $H_{2}O_{2}$, EDTA and SDS but was little inhibited by $N_{3}^{-}$. The absorption spectrum showed maximum peaks at 520 nm and 265 nm, but peak at 265 nm disappeared when treated with trace of cysteine. And atomic absorption spectroscopy indicated approximately 2 atoms of $Cu^{2+}$, $Zn^{2+}$ per mol enzyme. Thus, the result on this special properties showed that SOD was composed of Cu/Zn-form.
