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Purification of α-amylase by specific elution from anti-peptide antibodies.
- Source :
- Applied Microbiology & Biotechnology; May1997, Vol. 47 Issue 5, p521-524, 4p
- Publication Year :
- 1997
-
Abstract
- Chimeric α-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 α-amylase was adsorbed by the antibody against the peptide corresponding to the C-terminal region of target α-amylase, and specifically eluted by the eluent containing the antigen peptide used for immunization. A low concentration of the peptide could competitively elute adsorbed α-amylase, and the rate-limiting step of the elution was mass transfer of desorbed α-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. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 01757598
- Volume :
- 47
- Issue :
- 5
- Database :
- Complementary Index
- Journal :
- Applied Microbiology & Biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 49946865
- Full Text :
- https://doi.org/10.1007/s002530050966