Linked Life Data

7635150

Source:http://linkedlifedata.com/resource/pubmed/id/7635150

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1995-9-8
pubmed:abstractText
Streptolysin O is a member of a family of membrane-damaging toxins that bind to cell membranes containing cholesterol and then polymerize to form large pores. We have examined the kinetics of toxin action using 125I-labelled streptolysin O. Binding of toxin monomers to membranes displays first-order kinetics and is reversible; the rate of desorption from red cells shows a marked dependence on temperature. To study oligomerization, toxin was bound to erythrocytes at 0 degrees C. Oligomer formation was then triggered by a sudden temperature shift and stopped by solubilization of membranes with deoxycholate. While at moderately high streptolysin O concentrations oligomerization behaves as a reaction of second order, the kinetic pattern changes with increasing toxin concentration. We show that this can be accounted for by the assumption of a two-step reaction mechanism: two membrane-bound monomers first associate into a start complex, which then is rapidly extended by the sequential addition of further monomers up to the final oligomer size.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
231
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
388-95
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1995
pubmed:articleTitle
Kinetics of streptolysin O self-assembly.
pubmed:affiliation
Institute of Medical Microbiology, University of Mainz, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't