Linked Life Data

7703973

Source:http://linkedlifedata.com/resource/pubmed/id/7703973

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
1995-5-8
pubmed:abstractText
The binding properties of Sudlow's site-specific drugs to glycosylated bovine serum albumin (G-BSA) (1.25 mol glucose per mol of albumin) have been investigated using the circular dichroism (CD) method. Site I-specific drugs, phenylbutazone and warfarin, and site II-specific drugs, flufenamic acid and ibuprofen, were used. The induced ellipticities of phenylbutazone, flufenamic acid and ibuprofen-G-BSA complexes diminished and those of warfarin complex were enhanced in comparison with those for the intact bovine serum albumin (BSA) complexes. These CD change suggests that the glycosylation of BSA at the primary modification site influences the binding properties of the site-specific drugs to serum albumin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0918-6158
pubmed:author
pubmed:issnType
Print
pubmed:volume
17
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1505-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Drug binding properties of glycosylated bovine serum albumin as measured by circular dichroism.
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Kinki University, Osaka, Japan.
pubmed:publicationType
Journal Article, Comparative Study