Linked Life Data

9667024

Source:http://linkedlifedata.com/resource/pubmed/id/9667024

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1998-9-21
pubmed:abstractText
The influence of glycosylation on the drug binding of human serum albumin (HSA) was studied using HSA containing different amounts and degrees of glycosylated HSA. The drugs used were furosemide, naproxen, procaine, phenylbutazone, salicylic acid, sulphamethoxazole, tolbutamide and warfarin. The drug-HSA parameters (lognK) were measured by the ultrafiltration method, frontal analysis and a modified Hummel-Dreyer method. The modified Hummel-Dreyer method was the simplest method with high precision and required the smallest amounts of proteins. The lognK values were well correlated with the octanol-water partition coefficients; the correlation coefficients were over 0.95. The results suggested that hydrophobic interaction is the predominant force for the drug binding. The early stage of glycosylation of HSA did not significantly affect the drug-binding capacity. Generally, the binding affinity of HSA decreased, perhaps due to a conformational change or steric hindrance (except naproxen) when further glycosylation occurred.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0269-3879
pubmed:author
pubmed:issnType
Print
pubmed:volume
12
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
203-10
pubmed:dateRevised
2004-11-17
pubmed:meshHeading
pubmed:articleTitle
Influence of glycosylation on the drug binding of human serum albumin.
pubmed:affiliation
School of Pharmaceutical Sciences, Kitasato University, Tokyo, Japan.
pubmed:publicationType
Journal Article