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  • Title: Expression, purification and characterization of recombinant human beta-amyloid 1-42 in Pichia pastoris.
    Author: Shen M, Wang Q, Mu X, Xu H, Yan W.
    Journal: Protein Expr Purif; 2009 Feb; 63(2):84-8. PubMed ID: 18950715.
    Abstract:
    The human peptide rhA beta(1-42) was effectively produced through a novel expression system and purification procedure. The peptide rhA beta(1-42) was successfully expressed in Pichia pastoris, the methylotrophic yeast that has never been used as host. The cDNA encoding full-length hA beta(1-42) was synthesized with yeast bias codons and cloned into the pPICZ alpha A vector in frame with the yeast alpha-factor secretion signal under the transcriptional control of the AOX1 promoter and integrated into the secreting expression organism P. pastoris strain X33. Production of rhA beta(1-42) through fermentation was further optimized and scaled up in an 80 L fermentor. Secreted rhA beta(1-42) was purified using a two-step purification scheme: SP Sepharose ion exchange chromatography and source 30 RPC. The purification procedure is fast and efficient and reached a recovery of >93% without loss of activity. The purified rhA beta(1-42) was confirmed by Western blotting analysis and N-terminals amino sequencing analysis. This efficient and cost-effective expression system facilitates large-scale production and purification for recombinant rhA beta(1-42).
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