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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
|
pubmed:dateCreated |
1987-8-28
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pubmed:abstractText |
The A and B subunits of Shiga toxin were isolated by high performance liquid chromatography and their physicochemical properties were examined. The A subunit of Shiga toxin purified from culture supernatant was not nicked, but it could be nicked in vitro by trypsin. The isoelectric points of the A and B subunits were determined to be 8.2 and 5.8, respectively. Amino acid compositions of the two subunits were also determined. The isolated A and B subunits were reconstituted to form active holotoxin which showed lethal activity to mice which was similar to that of native Shiga toxin.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:issn |
0385-5600
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
31
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
189-97
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3302622-Amino Acids,
pubmed-meshheading:3302622-Animals,
pubmed-meshheading:3302622-Bacterial Toxins,
pubmed-meshheading:3302622-Chromatography, High Pressure Liquid,
pubmed-meshheading:3302622-Electrophoresis, Polyacrylamide Gel,
pubmed-meshheading:3302622-Isoelectric Point,
pubmed-meshheading:3302622-Mice,
pubmed-meshheading:3302622-Shiga Toxins,
pubmed-meshheading:3302622-Shigella dysenteriae,
pubmed-meshheading:3302622-Trypsin
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pubmed:year |
1987
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pubmed:articleTitle |
Physicochemical characterization of A and B subunits of Shiga toxin and reconstitution of holotoxin from isolated subunits.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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