J Korean Med Sci.  1987 Mar;2(1):65-70. 10.3346/jkms.1987.2.1.65.

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

• Cho MJ
• Chang WH
• Choi MS
• Kim IS
• Kang JS
• Park KH
• Kim HK
• Cha CY
• Chung HK
• Rhee KH

• KMID: 1421247
• DOI: http://doi.org/10.3346/jkms.1987.2.1.65

Abstract

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.

MeSH Terms

Animals
Antibodies, Monoclonal/biosynthesis/isolation & purification
Chromatography, Affinity/methods
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Enterotoxins/*isolation & purification
Enzyme-Linked Immunosorbent Assay
Escherichia coli/*analysis/pathogenicity
Humans
Mice
Mice, Inbred BALB C
Rabbits
Antibodies, Monoclonal
Enterotoxins