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通过与麦芽糖结合蛋白融合来促进外源肽在大肠杆菌中表达和纯化的载体。

Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein.

作者信息

di Guan C, Li P, Riggs P D, Inouye H

机构信息

New England BioLabs, Beverly, MA 01915.

出版信息

Gene. 1988 Jul 15;67(1):21-30. doi: 10.1016/0378-1119(88)90004-2.

Abstract

Vectors were constructed that allow foreign peptides to be expressed in Escherichia coli as fusion proteins. The peptides are fused to the C terminus of maltose-binding protein (MBP), which allows them to be purified by the MBP's affinity to cross-linked amylose (starch). The fusion protein can be directed to the periplasm by including the leader sequence from the phoA gene on the vector.

摘要

构建了一些载体,这些载体可使外源肽在大肠杆菌中作为融合蛋白表达。这些肽与麦芽糖结合蛋白(MBP)的C末端融合,这使得它们能够通过MBP与交联直链淀粉(淀粉)的亲和力来进行纯化。通过在载体上包含来自phoA基因的前导序列,融合蛋白可以被引导至周质。

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