Recovery and purification of recombinant 503 antigen of Leishmania infantum chagasi using expanded bed adsorption chromatography
Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health problem in many areas of the world. However, there is currently no vaccine for human use. The aim of this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified...
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| Hoofdauteurs: | , , , , , , |
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| Formaat: | article |
| Taal: | English |
| Gepubliceerd in: |
Elsevier
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| Onderwerpen: | |
| Online toegang: | https://repositorio.ufrn.br/handle/123456789/32482 |
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| Samenvatting: | Visceral leishmaniasis, a disease caused by Leishmania infantum chagasi, represents a major public health
problem in many areas of the world. However, there is currently no vaccine for human use. The aim of
this work was to purify the 503 antigen of Leishmania i. chagasi directly from unclarified Escherichia coli
feedstock through expanded bed adsorption (EBA) chromatography. Batch experiments were performed
to optimize the adsorption and elution conditions of the antigen onto a STREAMLINETM Chelating resin
using two central composite rotatable designs (CCRD). The results showed that the optimal binding con-
ditions of the 503 antigen were pH 8.0 in the presence of 2.4 M NaCl. For the elution of the target protein,
the optimized conditions included the presence of 600.0 mM imidazole. The adsorption isothermal data
of the 503 antigen were fitted to the Langmuir adsorption isotherm. The EBA experiment successfully
recovered 59.2% of the 503 antigen from the unclarified E. coli homogenate with a purification factor of
6.0 |
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