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Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.

Heat-labile enterotoxin (LT) was purified from an enterotoxigenic Escherichia coli 015H11 of human origin. The purification steps included French pressure cell disruption of the bacteria, salting-out, DEAE-Sephacel on chromatography. Application of this procedure resulted in a 95.1-fold purification...

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Detalles Bibliográficos
Autores principales: Cho, M. J., Chang, W. H., Choi, M. S., Kim, I. S., Kang, J. S., Park, K. H., Kim, H. K., Cha, C. Y., Chung, H. K., Rhee, K. H.
Formato: Texto
Lenguaje:English
Publicado: Korean Academy of Medical Sciences 1987
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053640/
https://www.ncbi.nlm.nih.gov/pubmed/3077605
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author Cho, M. J.
Chang, W. H.
Choi, M. S.
Kim, I. S.
Kang, J. S.
Park, K. H.
Kim, H. K.
Cha, C. Y.
Chung, H. K.
Rhee, K. H.
author_facet Cho, M. J.
Chang, W. H.
Choi, M. S.
Kim, I. S.
Kang, J. S.
Park, K. H.
Kim, H. K.
Cha, C. Y.
Chung, H. K.
Rhee, K. H.
author_sort Cho, M. J.
collection PubMed
description Heat-labile enterotoxin (LT) was purified from an enterotoxigenic Escherichia coli 015H11 of human origin. The purification steps included French pressure cell disruption of the bacteria, salting-out, DEAE-Sephacel on chromatography. Application of this procedure resulted in a 95.1-fold purification of LT with a yield of 19.9% as determined by rabbit ileal loop assay. The final LT preparation showed only one protein-staining band on polyacrylamide gel electrophoresis, indicating that the purified LT was homogeneous.
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spelling pubmed-30536402011-03-16 Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography. Cho, M. J. Chang, W. H. Choi, M. S. Kim, I. S. Kang, J. S. Park, K. H. Kim, H. K. Cha, C. Y. Chung, H. K. Rhee, K. H. J Korean Med Sci Research Article Heat-labile enterotoxin (LT) was purified from an enterotoxigenic Escherichia coli 015H11 of human origin. The purification steps included French pressure cell disruption of the bacteria, salting-out, DEAE-Sephacel on chromatography. Application of this procedure resulted in a 95.1-fold purification of LT with a yield of 19.9% as determined by rabbit ileal loop assay. The final LT preparation showed only one protein-staining band on polyacrylamide gel electrophoresis, indicating that the purified LT was homogeneous. Korean Academy of Medical Sciences 1987-03 /pmc/articles/PMC3053640/ /pubmed/3077605 Text en
spellingShingle Research Article
Cho, M. J.
Chang, W. H.
Choi, M. S.
Kim, I. S.
Kang, J. S.
Park, K. H.
Kim, H. K.
Cha, C. Y.
Chung, H. K.
Rhee, K. H.
Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title_full Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title_fullStr Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title_full_unstemmed Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title_short Purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic Escherichia coli of human origin by monoclonal immunoaffinity chromatography.
title_sort purification of heat-labile enterotoxin from an enterotoxin from an enterotoxigenic escherichia coli of human origin by monoclonal immunoaffinity chromatography.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3053640/
https://www.ncbi.nlm.nih.gov/pubmed/3077605
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