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Purification and partial characterization of Mn superoxide dismutase from muscle tissue of the shrimp Macrobrachium nipponense

文献类型：期刊论文

作者Yao, CL; Wang, AL; Wang, WN; Sun, RY
刊名AQUACULTURE
出版日期2004-11-26
卷号241期号:1-4页码:621-631
关键词Superoxide Dismutase Purification Characterization Macrobrachium Nipponense Muscle
ISSN号0044-8486
DOI10.1016/j.aquaculture.2004.08.023
文献子类Article
英文摘要Superoxide dismutase (SOD; EC 1.15.1.1) is an enzyme that protects against oxidative stress from superoxide radicals in living cells. This enzyme had been isolated, purified and partially characterized from muscle tissue of the shrimp Macrobrachium nipponense. The purification was achieved by heat treatment, ammonium sulfate fractionated precipitation and column chromatograph on DEAE-cellulose 32. Some physiological and biochemical characterization of it was tested. The molecular weight of it was about 21.7 kDa, as judged by SDS-polyacrylamide gel electrophoresis. The purified enzyme had an absorption peak of 278 nm in ultraviolet region, and the enzyme remained stable at 25-45 degreesC within 90 min. However, it was rapidly inactivated at higher temperature. Treatment of the enzyme with 1 mM ZnCl2, SDS and 1 mM or 10 mM mercaptoethanol showed some increasing activity. However, the enzyme activity was obviously inhibited by 10 mM CaCl2, CuSO4, ZnCl2 and 1 mM CaCl2 and 10 mM K2Cr2O7. SOD activity did not show significantly variation after incubated with 1 mM CaCl2, EDTA and 10 MM SDS. The enzyme was insensitive to cyanide and contained 1.03 +/- 0.14 atoms of manganese per subunit shown in atomic absorption spectroscopy, which revealed that purified SOD was Mn superoxide dismutase. (C) 2004 Elsevier B.V. All rights reserved.; Superoxide dismutase (SOD; EC 1.15.1.1) is an enzyme that protects against oxidative stress from superoxide radicals in living cells. This enzyme had been isolated, purified and partially characterized from muscle tissue of the shrimp Macrobrachium nipponense. The purification was achieved by heat treatment, ammonium sulfate fractionated precipitation and column chromatograph on DEAE-cellulose 32. Some physiological and biochemical characterization of it was tested. The molecular weight of it was about 21.7 kDa, as judged by SDS-polyacrylamide gel electrophoresis. The purified enzyme had an absorption peak of 278 nm in ultraviolet region, and the enzyme remained stable at 25-45 degreesC within 90 min. However, it was rapidly inactivated at higher temperature. Treatment of the enzyme with 1 mM ZnCl2, SDS and 1 mM or 10 mM mercaptoethanol showed some increasing activity. However, the enzyme activity was obviously inhibited by 10 mM CaCl2, CuSO4, ZnCl2 and 1 mM CaCl2 and 10 mM K2Cr2O7. SOD activity did not show significantly variation after incubated with 1 mM CaCl2, EDTA and 10 MM SDS. The enzyme was insensitive to cyanide and contained 1.03 +/- 0.14 atoms of manganese per subunit shown in atomic absorption spectroscopy, which revealed that purified SOD was Mn superoxide dismutase. (C) 2004 Elsevier B.V. All rights reserved.
学科主题Fisheries ; Marine & Freshwater Biology
URL标识查看原文
语种英语
WOS记录号WOS:000225070700044
公开日期2010-12-22
源URL[http://ir.qdio.ac.cn/handle/337002/3237]  
专题海洋研究所_实验海洋生物学重点实验室
作者单位1.S China Normal Univ, Coll Life Sci, Guangzhou 510631, Peoples R China
2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao 266071, Peoples R China
3.Hebei Univ, Coll Life Sci, Baoding 071002, Peoples R China
4.Chinese Acad Sci, Grad Sch, Beijing 100089, Peoples R China
推荐引用方式
GB/T 7714		 Yao, CL,Wang, AL,Wang, WN,et al. Purification and partial characterization of Mn superoxide dismutase from muscle tissue of the shrimp Macrobrachium nipponense[J]. AQUACULTURE,2004,241(1-4):621-631.
APA Yao, CL,Wang, AL,Wang, WN,&Sun, RY.(2004).Purification and partial characterization of Mn superoxide dismutase from muscle tissue of the shrimp Macrobrachium nipponense.AQUACULTURE,241(1-4),621-631.
MLA Yao, CL,et al."Purification and partial characterization of Mn superoxide dismutase from muscle tissue of the shrimp Macrobrachium nipponense".AQUACULTURE 241.1-4(2004):621-631.

入库方式： OAI收割

来源：海洋研究所

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