Linked Life Data

7660369

Source:http://linkedlifedata.com/resource/pubmed/id/7660369

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1995-10-4
pubmed:abstractText
Thermostable direct hemolysin (TDH) produced by Vibrio parahaemolyticus was iodinated using chloramine T. The 125I-labeled TDH retained up to 80% of the activity of intact toxin. The binding of 125I-TDH to rabbit erythrocytes was inhibited by addition of nonlabeled TDH. The binding of 125I-TDH to rabbit erythrocytes was completed in the 1st or 2nd min of incubation at 37 degrees C in contrast to that at 4 degrees C. 125I-TDH, which cannot lyse horse erythrocytes as does intact TDH, bound to horse erythrocytes as to those of rabbit. The dissociation constants (KD) derived Scatchard plots were 2.85, 4.39, 4.33 and 5.35 x 10-8M for rabbit, horse, human and sheep erythrocytes, respectively. The lytic sensitivity of various erythrocytes to TDH showed no relationship to the binding capacity.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:volume
33
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
651-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
The binding of Vibrio parahaemolyticus 125I-labeled thermostable directhemolysin to erythrocytes.
pubmed:affiliation
Department of Bacterial Infections, Osaka University, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't