Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1976-6-2
pubmed:abstractText
Enterotoxin, a diarrhea-inducing protein elaborated by pathogenic Escherichia coli strains, was isolated from the supernate of fermenter cultures of E. coli strain P263, a porcine enteropathogen. Purification involved chromatography and preparative isotachophoresis. The resulting product appeared to be pure according to immunoelectrophoretic, disc electrophoretic, ultracentrifugal, and immunologic criteria. The enterotoxin had an apparent molecular weight of 102,000 daltons, and its isoelectric point was 6.90. The isolated product was active in inducing experimental diarrhea in adult rabbits and piglets. In small dosage it also elicited a drastic increase in adenylate cyclase activity in broken-cell preparations of cat heart tissue. The enterotoxin activity was acid labile and was destroyed by heat (65 C for 30 min). It is suggested that the heat-stable enterotoxin was derived from heat-labile enterotoxin by complexing with endotoxin or with capsular material in the culture supernatant. The antigenic relations between the heat-labile enterotoxins of enteropathogenic E. coli strains of different serological types and different host adaptations, as well as between the E. coli enterotoxin and that of Vibrio cholerae, were investigated.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0022-1899
pubmed:author
pubmed:issnType
Print
pubmed:volume
133 Suppl
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
142-56
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1976
pubmed:articleTitle
Escherichia coli enterotoxin: purification, partial characterization, and immunological observations.
pubmed:publicationType
Journal Article