Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein.
摘要：
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.
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关键词：
Ap ampicillin ampicillin bp base pair(s base pair(s Δ deletion deletion Cm chloramphenicol chloramphenicol dNTP any of the four deoxynucleotide triphosphates any of the four deoxynucleotide triphosphates
DOI：
10.1016/0378-1119(88)90004-2
被引量：
年份：
1988
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