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王金星
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期刊论文
High level expression, puriWcation, and characterization of the shrimp antimicrobial peptide, Ch-penaeidin, in Pichia pastoris
Protein Expression and PuriWcation 39(2005)144-151，-0001，（）：
Penaeidins, members of a new family of antimicrobial peptides constitutively produced and stored in the haemocytes of penaeid shrimp, display antimicrobial activity against bacteria, and fungi. Here, a DNA sequence encoding the mature Ch-penaeidin peptide was cloned into the pPIC9K vector and transformed into Pichia pastoris. The transformed cells were screened for multi-copy plasmids using increasing concentrations of G418. Positive colonies carrying chromosomal integrations of the Chp gene were identiWed by phenotype and PCR. When transformed cells were induced with methanol, SDS-PAGE and Western blotting revealed the production of a
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