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 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.
Cho
M J
MJ
Department of Microbiology and Biochemistry, College of Medicine, Seoul National University, Korea.
Chang
W H
WH
Choi
M S
MS
Kim
I S
IS
Kang
J S
JS
Park
K H
KH
Kim
H K
HK
Cha
C Y
CY
Chung
H K
HK
Rhee
K H
KH
D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis / Q000302:isolation & purification; D002846:Chromatography, Affinity / Q000379:methods; D002850:Chromatography, Gel; D004591:Electrophoresis, Polyacrylamide Gel; D004768:Enterotoxins / Q000302:isolation & purification*; D004797:Enzyme-Linked Immunosorbent Assay; D004926:Escherichia coli / Q000032:analysis* / Q000472:pathogenicity; D006801:Humans; D051379:Mice; D008807:Mice, Inbred BALB C; D011817:Rabbits
D000911:Antibodies, Monoclonal; D004768:Enterotoxins