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Purification of recombinant α-amylase by immunoaffinity chromatography with anti-peptide antibody
- Source :
- Applied Microbiology and Biotechnology. 43:871-876
- Publication Year :
- 1995
- Publisher :
- Springer Science and Business Media LLC, 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 :
- Recombinant Fusion Proteins
Molecular Sequence Data
Peptide
Saccharomyces cerevisiae
Applied Microbiology and Biotechnology
Antibodies
Chromatography, Affinity
law.invention
Affinity chromatography
law
Amino Acid Sequence
Amylase
chemistry.chemical_classification
Chromatography
biology
Oryza
General Medicine
Yeast
Amino acid
Isoenzymes
Enzyme
chemistry
Biochemistry
Fermentation
Recombinant DNA
biology.protein
alpha-Amylases
Antibody
Oligopeptides
Biotechnology
Subjects
Details
- ISSN :
- 14320614 and 01757598
- Volume :
- 43
- Database :
- OpenAIRE
- Journal :
- Applied Microbiology and Biotechnology
- Accession number :
- edsair.doi.dedup.....a81595c17be4bc6b7c0db9c0f9fd32be