Linked Life Data

3094925

Source:http://linkedlifedata.com/resource/pubmed/id/3094925

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1986-12-16
pubmed:abstractText
Hemolysin produced by Vibrio hollisae (Vh-rTDH), which is related to the thermostable direct hemolysin (Vp-TDH) of Vibrio parahaemolyticus, was studied. Vh-rTDH was purified by successive column chromatographies on diethylaminoethyl-cellulose and an immunoaffinity column coupled with anti Vp-TDH immunoglobulin. The purified toxin was homogeneous, as demonstrated by conventional and sodium dodecyl sulfate--polyacrylamide gel electrophoresis (PAGE). The molecular weight of Vh-rTDH was slightly smaller than that of Vp-TDH, as determined by sodium dodecyl sulfate--slab gel electrophoresis. Conventional PAGE also showed a difference between Vh-rTDH and Vp-TDH. Vp-TDH and Vh-rTDH showed different lytic activities on erythrocytes from various animals, in particular chicken, sheep, and calf. The hemolytic activity of Vh-rTDH was heat labile when heated at 70 degrees C for 10 min, unlike Vp-TDH. Immunological cross-reactivity between Vh-rTDH and Vp-TDH was demonstrated by both the Ouchterlony test and neutralization test.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0008-4166
pubmed:author
pubmed:issnType
Print
pubmed:volume
32
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
632-6
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1986
pubmed:articleTitle
Purification and partial characterization of a Vibrio hollisae hemolysin that relates to the thermostable direct hemolysin of Vibrio parahaemolyticus.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't