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An Improved Method for the Purification and Refolding of r56-kDa Proteins from Gilliam and Kato strains ofOrientia tsutsugamushi
- Source :
- Annals of the New York Academy of Sciences. 990:375-385
- Publication Year :
- 2003
- Publisher :
- Wiley, 2003.
-
Abstract
- The immunodominant 56kDa outer membrane antigens from Orientia tsutsugamushi Kato and Gilliam strains were expressed as inclusion bodies (IBs) in E. coli. The IBs were purified and properly refolded with modifications of a previous procedure used for the production of Karp strain r56 antigen. A mixture of these three r56 proteins exhibited both high sensitivity and specificity for detection of O. tsutsugamushi antibodies by ELISA.
- Subjects :
- Protein Denaturation
Protein Folding
Orientia tsutsugamushi
Enzyme-Linked Immunosorbent Assay
Improved method
General Biochemistry, Genetics and Molecular Biology
Inclusion bodies
Microbiology
Bacterial Proteins
History and Philosophy of Science
Antigen
Cloning, Molecular
Chromatography, High Pressure Liquid
DNA Primers
Base Sequence
Strain (chemistry)
biology
Chemistry
General Neuroscience
bacterial infections and mycoses
biology.organism_classification
Molecular biology
Recombinant Proteins
Orientia tsutsugamushi Kato
Molecular Weight
Chromatography, Gel
biology.protein
Electrophoresis, Polyacrylamide Gel
Antibody
Bacterial outer membrane
Subjects
Details
- ISSN :
- 17496632 and 00778923
- Volume :
- 990
- Database :
- OpenAIRE
- Journal :
- Annals of the New York Academy of Sciences
- Accession number :
- edsair.doi.dedup.....8773c7d049189da948ecb7d97f9d0de3