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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1997-9-26
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pubmed:abstractText |
The interaction of 13 antibiotics with human serum albumin was studied by charge-transfer reversed-phase thin-layer chromatography in neutral, acidic, basic and ionic environments (NaCl and MgCl2) and the relative strength of interaction was calculated. The pH and the presence of mono- and divalent cations markedly influenced the strength of interaction. The capacity of antibiotics to interact with HSA also considerably depended on their chemical structure.
|
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
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pubmed:issn |
0021-9673
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
776
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
31-6
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pubmed:dateRevised |
2009-1-15
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pubmed:meshHeading |
pubmed-meshheading:9286075-Anti-Bacterial Agents,
pubmed-meshheading:9286075-Chemistry, Physical,
pubmed-meshheading:9286075-Chromatography, Thin Layer,
pubmed-meshheading:9286075-Humans,
pubmed-meshheading:9286075-Hydrogen-Ion Concentration,
pubmed-meshheading:9286075-Physicochemical Phenomena,
pubmed-meshheading:9286075-Protein Binding,
pubmed-meshheading:9286075-Serum Albumin,
pubmed-meshheading:9286075-Spectrophotometry, Ultraviolet
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pubmed:year |
1997
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pubmed:articleTitle |
Study of the binding of antibiotics to human serum albumin by charge-transfer chromatography.
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pubmed:affiliation |
Central Research Institute for Chemistry, Hungarian Academy of Sciences, Budapest, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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