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Purification of recombinant alpha-amylase by immunoaffinity chromatography with anti-peptide antibody.
- Source :
-
Applied microbiology and biotechnology [Appl Microbiol Biotechnol] 1995 Oct; Vol. 43 (5), pp. 871-6. - Publication Year :
- 1995
-
Abstract
- Adsorption characteristics of an anti-peptide antibody, obtained by immunization of eight amino acids in the C-terminal region of chimeric alpha-amylase of rice alpha-amylase isozymes, were studied by use of the chimeric enzyme and the peptide used for immunization. This anti-peptide antibody adsorbed the enzyme, as well as the peptide antigen, with sufficient affinity for immunoaffinity purification and was used for purification of the enzyme secreted from yeast cells. Chimeric alpha-amylase was purified by immunoaffinity chromatography to high purity in one step from the fermentation broth. One-third of the secreted enzyme was not adsorbed by the column of anti-peptide antibody because of processing in the C-terminal region.
- Subjects :
- Amino Acid Sequence
Antibodies
Fermentation
Isoenzymes immunology
Molecular Sequence Data
Oligopeptides immunology
Oryza enzymology
Recombinant Fusion Proteins isolation & purification
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
alpha-Amylases immunology
Chromatography, Affinity methods
alpha-Amylases isolation & purification
Subjects
Details
- Language :
- English
- ISSN :
- 0175-7598
- Volume :
- 43
- Issue :
- 5
- Database :
- MEDLINE
- Journal :
- Applied microbiology and biotechnology
- Publication Type :
- Academic Journal
- Accession number :
- 7576554
- Full Text :
- https://doi.org/10.1007/BF02431921