Product of the Schistosoma mansoni Glutathione Peroxidase Gene is a Selenium ContainingPhospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) Sharing MolecularWeight and Substrate Specificity WithIts Mammalian Counterpart  

Product of the Schistosoma mansoni Glutathione Peroxidase Gene is a Selenium Containing Phospholipid Hydroperoxide Glutathione Peroxidase (PHGPx) Sharing Molecular Weight and Substrate Specificity With Its Mammalian Counterpart

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作  者:MATILDE MAIORINO RAYMOND PIERCE AND LEOPOLD FLOHE (Dipartimento di Chimica Biologica, Universitd di Padova, Padova, Italy Reltion hote-parasite stratigies vaccinales, INSERM U167, Institut Pasteur, Lille Cedex, France Department of Physiological Chemistr 

出  处:《Biomedical and Environmental Sciences》1997年第2期209-213,共5页生物医学与环境科学(英文版)

摘  要:In the blood fluke Schistosoma mansoni a functionally active, monomeric, phospholipid hydroperoxide glutathione peroxidase (PHGPx) has been purified and characterized. This enzyme contains a catalytically active selenocysteine. The protein has been shown to be the product of a cloned gene, previously referred to as a glutathione peroxidase gene. S. mansoni PHGPx has been found 5 times more abundant in female than in male worm extract. As in vertebrate PHGPx, homology alignment indicates that the residues involved in the glutathione binding by the tetrameric cellular glutathione peroxidase are mutated in the S. mansoni enzyme. Thus, this aspect appears a landmark of the PHGPx-type of glutathione peroxidases,which might be of functional relevanceIn the blood fluke Schistosoma mansoni a functionally active, monomeric, phospholipid hydroperoxide glutathione peroxidase (PHGPx) has been purified and characterized. This enzyme contains a catalytically active selenocysteine. The protein has been shown to be the product of a cloned gene, previously referred to as a glutathione peroxidase gene. S. mansoni PHGPx has been found 5 times more abundant in female than in male worm extract. As in vertebrate PHGPx, homology alignment indicates that the residues involved in the glutathione binding by the tetrameric cellular glutathione peroxidase are mutated in the S. mansoni enzyme. Thus, this aspect appears a landmark of the PHGPx-type of glutathione peroxidases,which might be of functional relevance

关 键 词:Sharing MolecularWeight and Substrate Specificity WithIts Mammalian Counterpart Gene Product of the Schistosoma mansoni Glutathione Peroxidase Gene is a Selenium ContainingPhospholipid Hydroperoxide Glutathione Peroxidase PHGPX 

分 类 号:R383.24[医药卫生—医学寄生虫学] Q51[医药卫生—基础医学]

 

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