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  • Title: Purification of alpha-amylase by specific elution from anti-peptide antibodies.
    Author: Katoh S, Terashima M, Miyaoku K.
    Journal: Appl Microbiol Biotechnol; 1997 May; 47(5):521-4. PubMed ID: 9210341.
    Abstract:
    Chimeric alpha-amylase, produced by recombinant yeast cells, was purified by immunoaffinity chromatography by use of an anti-peptide antibody and an eluent containing an antigen peptide. Chimeric alpha-amylase was adsorbed by the antibody against the peptide corresponding to the C-terminal region of target alpha-amylase, and specifically eluted by the eluent containing the antigen peptide used for immunization. A low concentration of the peptide could competitively elute adsorbed alpha-amylase, and the rate-limiting step of the elution was mass transfer of desorbed alpha-amylase. With this specific method, target proteins can be effectively eluted, and highly purified under mild conditions, from the antibody ligand showing a high-affinity for the adsorption step
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