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首页> 外文期刊>Protein Expression and Purification >Purification and characterization of Delta 3Trx-1, a splicing variant of human thioredoxin-1 lacking exon 3
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Purification and characterization of Delta 3Trx-1, a splicing variant of human thioredoxin-1 lacking exon 3

机译：缺少外显子3的人类硫氧还蛋白1的剪接变体Delta 3Trx-1的纯化和表征

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摘要

Thioredoxins comprise a growing family of proteins that function as general protein-disulfide reductases and are maintained in their reduced active form by the flavoenzyme thioredoxin reductase. Human Trx-1 is mainly a cytosolic protein, although it has been shown to translocate into the nucleus upon certain stimuli and can also be secreted. We report here the expression and characterization of Delta3Trx-1, a splicing variant of human Trx-1, lacking exon 3, which spans from residues 44 to 63 in the wild-type protein. Structure-based prediction of this splicing form indicates that A3Trx-1 lacks helix alpha2 and strand beta3, which are implicated in substrate positioning and three-dimensional stabilization of the active site residues. Recombinant human Delta3Trx-1 is recognized by polyclonal antibodies raised against full-length human Trx-1. However, Delta3Trx-1 retains no enzymatic activity either with DTT or thioredoxin reductase and NADPH as reducing systems. Delta3Trx-1 competes with full-length Trx-1 for the interaction with thioredoxin reductase. The absence of helix alpha2 and strand beta3 in A3Trx-1 is consistent with the lack of enzymatic activity and its potential dominant negative properties. (C) 2002 Elsevier Science (USA). All rights reserved. [References: 30]
机译：硫氧还蛋白包含越来越多的蛋白质家族，这些蛋白质起一般的蛋白质-二硫键还原酶的作用，并通过黄素酶硫氧还蛋白还原酶保持其还原活性形式。人Trx-1主要是胞质蛋白，尽管已显示它在某些刺激下可转移到细胞核中，也可以被分泌。我们在这里报告Delta3Trx-1的表达和特征，它是人Trx-1的剪接变体，缺少外显子3，该外显子从野生型蛋白的第44位残基到第63位残基。这种剪接形式的基于结构的预测表明，A3Trx-1缺少螺旋α2和链beta3，这与底物定位和活性位点残基的三维稳定有关。重组人Delta3Trx-1被针对全长人Trx-1的多克隆抗体识别。但是，无论是DTT还是硫氧还蛋白还原酶和NADPH作为还原系统，Delta3Trx-1均不保留酶活性。 Delta3Trx-1与全长Trx-1竞争与硫氧还蛋白还原酶的相互作用。 A3Trx-1中不存在螺旋α2和链beta3与缺乏酶活性及其潜在的显性负性特性相一致。 （C）2002 Elsevier Science（美国）。版权所有。 [参考：30]

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