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PMID: 103838 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Purification of heat-labile enterotoxin from four Escherichia coli strains by affinity immunoadsorbent: evidence for similar subunit structure.

Infection and immunity ·Vol. 22 ·No. 3 ·1978-12-00 ·Pages 852-60

Dafni Z, Sack RB, Craig JP

Abstract

A single-step method for the purification of heat-labile enterotoxin of Escherichia coli is described. The method involves an affinity immunoadsorbent made with antiserum to cholera toxin. Crude toxin preparations of three human and one porcine enterotoxinogenic strains of E. coli were purified on this immunoadsorbent, and the elution products suggest that the toxin molecule is composed of subunits. One kind of subunit shared by these four strains showed similar mobility of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, close antigenic relationship, and an antigen in common with cholera enterotoxin.

MeSH Terms
Antigens, Bacterial/analysis Bacterial Toxins/analysis,isolation & purification Chromatography, Gel Electrophoresis, Polyacrylamide Gel Enterotoxins/analysis,immunology,isolation & purification Escherichia coli/analysis Hot Temperature Immunodiffusion Immunosorbent Techniques Molecular Weight
Chemicals
Antigens, Bacterial Bacterial Toxins Enterotoxins
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Dafni Z
Sack R B
Craig J P
References (19)
19 references, click to expand
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Article Info
Journal
Infection and immunity
Abbr.
Infect Immun
ISSN
0019-9567
DOI
10.1128/iai.22.3.852-860.1978
Published
1978-12-00
Pages
852-60
Language
English
Region
United States
NLM ID
0246127
PMCID
PMC422237
Subset
IM
External Links
PubMed source DOI: 10.1128/iai.22.3.852-860.1978 PMC Full Text View journal details
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