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題名 | Purification and Characterization of Black Porgy Muscle Cu/Zn Superoxide Dismutase=黑鯛銅鋅型超氧歧化酶之純化及其性質之研究 |
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作者 | 林棋財; 李棟樑; 段國仁; 蘇仲卿; Lin, Chi-tsai; Lee, Tung-liang; Duan, Kow-jen; Su, Jong-ching; |
期刊 | 動物研究學刊 |
出版日期 | 20010400 |
卷期 | 40:2 2001.04[民90.04] |
頁次 | 頁84-90 |
分類號 | 383.2 |
語文 | eng |
關鍵詞 | 黑鯛; 銅鋅型超氧歧化酶; 熱穩定性; Black porgy; Acanthopagrus schlegeli; Cu/Zn superoxide dismutase; Thermal stability; |
中文摘要 | 生物體內超氧歧化�t可當作對環境污染程度之生物指標,顯見其重要性。以黑鯛為材料,經測定其銅鋅型超氧歧化�t存在六種組織中,但心臟、肝臟及雄性生殖器同時亦含猛型超氧歧化�t。以其肌肉為材料,其粗抽取液經加熱及兩種管柱層析,可得到均質之純酵素。測得原態分子為33kDa,次單元體為15.85kDa,N端之胺酸為VLKAVCVLKGAGQTTGVV,比活性每毫克含3318單位,此�t對pH、蛋白質水解�t及80℃加熱處理均甚穩定。 |
英文摘要 | Superoxide dismutase (SOD) has been proposed to be used as a bioindicator for environmental impact assessment. From a survey of SOD activity in black porgy, Acanthopagrus schlegeli, we found that Cu/Zu SOD was distributed rather evenly in 6 tissues, and in addition, only heart, liver, and testis had Mn SOD. We purified Cu/Zn SOD from muscle to homogeneity by a procedure that includes heating at 65 ℃ and fractionation on 2 chromatographic columns. The molecular mass of the native enzyme was 33 kDa and that of the subunit mass, deduced from a cDNA sequence, was 15.85 kDa. Thus the native enzyme appeared to be a homodimer. It had an N-terminal sequence of VLKAVCVLKGAGQTTGVV. The specific activity was 3318 u/mg, The enzyme had a broad optimum pH range of 5.8 to 11.2 and was resistant both to proteolysis by trypsin and chymotrypsin and to heat denaturation. The thermal inactivation rate constant of the enzyme at 80 ℃ was -0.0237 min and the half life for inactivation was 27.8 min. |
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