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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45590

Title: Purification and characterization of the copper/zinc-superoxide dismutase from black porgy.
Authors: Chi-Tsai Lin;T.-L. Lee;K.-J. Duan;J.-C. Su
Contributors: 國立臺灣海洋大學:生命科學系
Date: 2001
Issue Date: 2018-03-27T08:18:07Z
Publisher: Zoological studies
Abstract: Abstract: Purification and characterization of black porgy muscle Cu/Zn superoxide dismutase. Zoological Studies 40(2): 84-90. 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/Zn 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 °C 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 °C was -0.0237 min-1 and the half life for inactivation was 27.8 min.
Relation: 40(2)
URI: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/45590
Appears in Collections:[生命科學系] 期刊論文

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