从胎盘净化,氨基酸序列、结构比较和cDNA克隆人类glutaredoxin。
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帕迪拉CA, Martinez-Galisteo E, Barcena是的,Spyrou G,霍蒙格林
从胎盘净化,氨基酸序列、结构比较和cDNA克隆人类glutaredoxin。
欧元。1995 1月15日,227 (2):27-34。
- PubMed ID
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7851394 (在PubMed]
- 文摘
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Glutaredoxin通常是glutathione-dependent氢供体的核苷酸还原酶还会刺激总谷胱甘肽(GSH) -disulfide-oxidoreduction反应NADPH和谷胱甘肽还原酶的存在。从人类胎盘Glutaredoxin纯化同质性,根据SDS /页面和(12 kDa)。净化被活动监测与羟乙基二硫作为衬底。的π值glutaredoxin能源论坛获得的合作;蛋白质的π从7.3完全减少状态转移到9.0后的氧化状态,治疗过量的羟乙基二硫化物。glutaredoxin准备显示GSH-dependent氢供体与鼠标核苷酸还原酶重组活动,它表现出dehydroascorbate还原酶活性以及hydroxyethyl-disulfide-reducing活动。氨基酸序列(残留3 - 104)glutaredoxin是由肽测序和残留1、2和105年cDNA序列分析。glutaredoxin序列由经典的活性部位为glutaredoxins -Cys22-Pro-Tyr-Cys25 -和另外三个half-cystine残留物;其中两个在78年和82年的位置。序列是类似于其他已知的哺乳动物glutaredoxins身份(大约80%),与一个额外的半胱氨酸残基等重要的差异(Cys7)和没有残留物。 The sequence of human glutaredoxin was compared to that of Escherichia coli glutaredoxin with known three-dimensional structure in solution to identify conserved residues and predict a structure from alignment. In particular the GSH-binding site of glutaredoxin was conserved between all molecules. A cDNA that encodes the entire glutaredoxin gene (grx) and flanking sequences was isolated from a human spleen cDNA library. The nucleotide sequence of this cDNA (0.8 kb) was determined, including the complete grx gene.