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本文引用的文献

1
Redox and antioxidant systems of the malaria parasite Plasmodium falciparum.恶性疟原虫的氧化还原与抗氧化系统
Mol Microbiol. 2004 Sep;53(5):1291-305. doi: 10.1111/j.1365-2958.2004.04257.x.
2
Linked thioredoxin-glutathione systems in platyhelminths.扁形动物中的硫氧还蛋白-谷胱甘肽连接系统
Trends Parasitol. 2004 Jul;20(7):340-6. doi: 10.1016/j.pt.2004.05.002.
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Innate immunity to malaria.疟疾的天然免疫
Nat Rev Immunol. 2004 Mar;4(3):169-80. doi: 10.1038/nri1311.
4
Protein measurement with the Folin phenol reagent.使用福林酚试剂进行蛋白质测定。
J Biol Chem. 1951 Nov;193(1):265-75.
5
Thioredoxin reductase is essential for the survival of Plasmodium falciparum erythrocytic stages.
J Biol Chem. 2002 Jul 19;277(29):25970-5. doi: 10.1074/jbc.M203539200. Epub 2002 May 9.
6
The thioredoxin system of the malaria parasite Plasmodium falciparum. Glutathione reduction revisited.恶性疟原虫的硫氧还蛋白系统。重新审视谷胱甘肽还原作用。
J Biol Chem. 2000 Dec 22;275(51):40180-6. doi: 10.1074/jbc.M007633200.
7
Mitochondrial thioredoxin reductase in bovine adrenal cortex its purification, properties, nucleotide/amino acid sequences, and identification of selenocysteine.牛肾上腺皮质中的线粒体硫氧还蛋白还原酶:其纯化、性质、核苷酸/氨基酸序列及硒代半胱氨酸的鉴定
Eur J Biochem. 1999 Aug;264(1):74-84. doi: 10.1046/j.1432-1327.1999.00578.x.
8
The malaria parasite supplies glutathione to its host cell--investigation of glutathione transport and metabolism in human erythrocytes infected with Plasmodium falciparum.疟原虫向其宿主细胞提供谷胱甘肽——对感染恶性疟原虫的人类红细胞中谷胱甘肽转运和代谢的研究。
Eur J Biochem. 1997 Dec 15;250(3):670-9. doi: 10.1111/j.1432-1033.1997.00670.x.
9
Glutathione reductase and glutamate dehydrogenase of Plasmodium falciparum, the causative agent of tropical malaria.
Eur J Biochem. 1996 Jan 15;235(1-2):345-50. doi: 10.1111/j.1432-1033.1996.00345.x.
10
Origin of reactive oxygen species in erythrocytes infected with Plasmodium falciparum.恶性疟原虫感染红细胞中活性氧的来源。
Mol Biochem Parasitol. 1993 Oct;61(2):231-41. doi: 10.1016/0166-6851(93)90069-a.

谷胱甘肽还原酶和硫氧还蛋白还原酶:来自伯氏疟原虫的新型抗氧化酶。

Glutathione reductase and thioredoxin reductase: novel antioxidant enzymes from Plasmodium berghei.

作者信息

Kapoor Gaurav, Banyal Harjeet Singh

机构信息

Laboratory of Parasitology and Immunology, Department of Biosciences, Himachal Pradesh University, Shimla 171005, India.

出版信息

Korean J Parasitol. 2009 Dec;47(4):421-4. doi: 10.3347/kjp.2009.47.4.421. Epub 2009 Dec 1.

DOI:10.3347/kjp.2009.47.4.421
PMID:19967095
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC2788726/
Abstract

Malaria parasites adapt to the oxidative stress during their erythrocytic stages with the help of vital thioredoxin redox system and glutathione redox system. Glutathione reductase and thioredoxin reductase are important enzymes of these redox systems that help parasites to maintain an adequate intracellular redox environment. In the present study, activities of glutathione reductase and thioredoxin reductase were investigated in normal and Plasmodium berghei-infected mice red blood cells and their fractions. Activities of glutathione reductase and thioredoxin reductase in P. berghei-infected host erythrocytes were found to be higher than those in normal host cells. These enzymes were mainly confined to the cytosolic part of cell-free P. berghei. Full characterization and understanding of these enzymes may promise advances in chemotherapy of malaria.

摘要

疟原虫在其红细胞阶段借助重要的硫氧还蛋白氧化还原系统和谷胱甘肽氧化还原系统来适应氧化应激。谷胱甘肽还原酶和硫氧还蛋白还原酶是这些氧化还原系统的重要酶类,有助于疟原虫维持适当的细胞内氧化还原环境。在本研究中,对正常和感染伯氏疟原虫的小鼠红细胞及其组分中的谷胱甘肽还原酶和硫氧还蛋白还原酶活性进行了研究。发现感染伯氏疟原虫的宿主红细胞中谷胱甘肽还原酶和硫氧还蛋白还原酶的活性高于正常宿主细胞中的活性。这些酶主要局限于无细胞伯氏疟原虫的胞质部分。对这些酶的全面表征和理解可能为疟疾化疗带来进展。