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Plasmid, Vol. 45, Iss. 2, 2001-03 ,pp. : 101-113

Academic Press

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Efficient Secretion of Biologically Active Recombinant OB Protein (Leptin) in Escherichia coli, Purification from the Periplasm and Characterization

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Development of a simple method for the recovery of recombinant proteins from the Escherichia coli periplasm

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Construction and application of the vectors to identify genes encoding exported proteins of Escherichia coli

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A Versatile Prokaryotic Cloning Vector with Six Dual Restriction Enzyme Sites in the Polylinker Facilitates Efficient Subcloning into Vectors with Unique Cloning Sites

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