di Guan C, Li P, Riggs P D, Inouye H
New England BioLabs, Beverly, MA 01915.
Gene. 1988 Jul 15;67(1):21-30. doi: 10.1016/0378-1119(88)90004-2.
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.
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。