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Purification and partial characterization of glutathione transferase from the teleost Monopterus albus.

Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Research Abstract Details 

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  • Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Abstract Text:

    qing huangQing Huang,li liangLi Liang,tao weiTao Wei,daming zhangDaming Zhang,qing-yin zengQing-Yin Zeng,qing huangQing Huang,li liangLi Liang,tao weiTao Wei,daming zhangDaming Zhang,qing-yin zengQing-Yin Zeng,

    Glutathione transferases (GSTs) catalyze the transfer of glutathione to a variety of xenobiotic and toxic endogenous compounds. GSTs are phase II biotransformation enzymes and are proposed as biomarkers of environmental pollution. In this study, a cytosolic glutathione transferase (maGST) was purified from liver of the freshwater fish Monopterus albus by affinity chromatography. The maGST appeared to be a homodimer composed of two subunits each with a molecular weight of 26 kDa. This maGST showed high activity towards the substrates 1-chloro-2,4-dinitrobenzene (CDNB) and 7-chloro-4-nitrobenzo-2-oxa-1,3-diazole (NBD-Cl). Kinetic analysis with CDNB as substrate revealed a K(m) of 0.28 mM and V(max) of 15.68 mumol/min per mg of protein. It had maximum activity in the pH range 7.0-7.5, a broad optimum T(m) range of 30 degrees C-55 degrees C, and a high thermal stability with 77% of its initial activity at 45 degrees C. This high thermal stability of maGST could be related to the physiological adaptation of M. albus to high temperatures in tropical and subtropical environments.

    Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Publishing Authors By Initials

    q huangQ Huang,l liangL Liang,t weiT Wei,d zhangD Zhang,qy zengQY Zeng,q huangQ Huang,l liangL Liang,t weiT Wei,d zhangD Zhang,qy zengQY Zeng,

    For similar abstracts research abstracts see: abstracts research

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    Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Journal Published:

    PUBLICATION TYPE: Journal Article

    Journal: Comparative biochemistry and physiology. Toxicolog

    VOLUME: 147

    Page Numbers: 96-100

    Journal Abbreviation: Comp. Biochem. Physiol. C Toxi

    ISSN: 1532-0456

    DAY: 22

    MONTH: 08

    YEAR: 2007

    Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Information

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    LANGUAGE: eng

    NlmUniqueID: 100959500

    Purification and partial characterization of glutathione transferase from the teleost Monopterus albus. Keywords Mesh Terms:

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    Grant and Affiliation Information for Purification and partial characterization of glutathione transferase from the teleost Monopterus albus.

    AFFILIATION: State Key Laboratory of Systematic and Evolutionary Botany, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China; Graduate School, Chinese Academy of Sciences, Beijing 100049, China.

    Country: United States

    United States Research PublicationUnited States Research Publication

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    MEDLINETA: Comp Biochem Physiol C Toxicol

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