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首页> 外文期刊>Journal of bacteriology >Sites within gene lacZ of Escherichia coli for formation of active hybrid beta-galactosidase molecules.
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Sites within gene lacZ of Escherichia coli for formation of active hybrid beta-galactosidase molecules.

机译:大肠杆菌基因lacZ内用于形成活性杂合β-半乳糖苷酶分子的位点。

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摘要

We describe the genetic analysis of 21 Escherichia coli strains in which the amino-terminal sequence of beta-galactosidase has been removed and replaced by an amino-terminal sequence from one or another of the proteins involved in maltose transport. Genetic mapping of the lacZ end of these fused genes indicates that only those fusions in which fewer than 41 amino acids are removed from the amino-terminal sequence of beta-galactosidase result in enzymatically active molecules. Within the region between amino acid 17 and amino acid 41 there are at least four or five sites where enzymatically active hybrid proteins can be formed.
机译:我们描述了21个大肠杆菌菌株的遗传分析,其中β-半乳糖苷酶的氨基末端序列已被去除,并被一个或另一个参与麦芽糖运输的蛋白质的氨基末端序列取代。这些融合基因的lacZ末端的遗传图谱表明,只有那些从β-半乳糖苷酶的氨基末端序列中去除少于41个氨基酸的融合物才会产生酶活性分子。在氨基酸17和氨基酸41之间的区域内,存在至少四个或五个可以形成酶活性杂合蛋白的位点。

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