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文献和实验Recombinant Single Globin-Chain Expression and Purification
with methionine aminopeptidase (MAP) cDNA.
Expression of Recombinant Proteins with Uniform N-Termini
Heterologously expressed proteins in Escherichia coli may undergo unwanted N-terminal processing by methionine and proline aminopeptidases. To overcome this problem, we present a system where the gene of interest is cloned as a fusion
Thioredoxin and Related Proteins as Multifunctional Fusion Tags for Soluble Expression in E. coli
(1 ). Recombinant proteins produced in E. coli sometimes retain the N-terminal initiator methionine residue, as they may be a poor substrate for the host methionine aminopeptidase (2 ). In addition, individual purification schemes must be devised for each native
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