Strategies for the purification of intact and proteolytically-activated native and engineered heat-labile enterotoxins of Escherichia coli.
Ruston
S
S
Research School of Biosciences, University of Kent, Canterbury, UK.
Eaglestone
S
S
Webb
H
H
Hirst
T R
TR
D001427:Bacterial Toxins / Q000096:biosynthesis / Q000302:isolation & purification*; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004591:Electrophoresis, Polyacrylamide Gel; D004768:Enterotoxins / Q000096:biosynthesis / Q000302:isolation & purification*; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins; D005798:Genes, Bacterial; D008970:Molecular Weight; D016297:Mutagenesis, Site-Directed; D010957:Plasmids; D017354:Point Mutation; D015202:Protein Engineering; D011994:Recombinant Proteins / Q000096:biosynthesis / Q000302:isolation & purification*
D001427:Bacterial Toxins; D004768:Enterotoxins; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; C034151:heat stable toxin (E coli); C027538:heat-labile enterotoxin, E coli