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rdf:type |
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|
lifeskim:mentions |
|
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pubmed:issue |
2
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pubmed:dateCreated |
1991-8-8
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pubmed:abstractText |
A previously published computerized drop-weight technique for surface tension measurements, not involving the use of radioactively labelled compounds, has been applied to the study of detergent binding to proteins. The procedure is based on the observation that the protein-surfactant complex is no longer surface-active. As an example, the binding of Triton X-100 to bovine serum albumin has been studied, and the results were found to be in good agreement with those obtained through established but less convenient methods. Our procedure should be useful for measurements of detergent binding to biomembranes.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
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pubmed:status |
MEDLINE
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pubmed:issn |
0165-022X
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pubmed:author |
|
|
pubmed:issnType |
Print
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pubmed:volume |
22
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
129-33
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
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pubmed:articleTitle |
Binding of Triton X-100 to bovine serum albumin as studied by surface tension measurements.
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pubmed:affiliation |
Faculté des Sciences, Laboratoire de Chimie Générale I, Université Libre de Bruxelles, Belgium.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
|
