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首页> 外文期刊>Journal of bacteriology >Hybrid tryptophan synthase beta 2 proteins: apparent conservation of the beta-beta binding region of the beta monomer among enteric bacteria.
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Hybrid tryptophan synthase beta 2 proteins: apparent conservation of the beta-beta binding region of the beta monomer among enteric bacteria.

机译:杂合色氨酸合酶β2蛋白:肠细菌中β单体的β-β结合区的明显保守性。

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Purified borohydride-reduced tryptophan synthase beta 2 protein (EC 4.2.1.20) from Escherichia coli and purified native beta 2 protein from Serratia marcescens were mixed and dissociated in urea. Removal of the urea resulted in random reassociation of the reduced and native beta monomers, forming interspecies hybrid beta 2 molecules. Interspecies hybrid beta 2 protein molecules of the reciprocal composition were also formed. Interspecies hybrid reconstituted molecules were formed with approximately the same efficiency as intraspecies reconstituted molecules (reduced and native monomers from the same species) indicating no particular preference for reassembly. The data provide evidence that the structural region of interaction between the beta monomers necessary for dimerization is highly conserved in the enzymes from the two organisms examined.
机译:将来自大肠杆菌的纯化的硼氢化物还原的色氨酸合酶β2蛋白(EC 4.2.1.20)和来自粘质沙雷氏菌的纯化的天然β2蛋白混合并在尿素中解离。尿素的去除导致还原的和天然的β单体的随机重新缔合,形成种间杂合的β2分子。还形成了相互组成的种间杂合β2蛋白分子。种间杂交重组分子的形成效率与种内重组分子(相同物种的还原单体和天然单体)的效率大致相同,表明对重组没有特别的偏好。数据提供了证据,证明二聚化所必需的β单体之间相互作用的结构区域在所研究的两种生物的酶中高度保守。

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