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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2005-10-3
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pubmed:abstractText |
The binding of flunitrazepam (FNZP) by human alpha1-acid glycoprotein (hAGP) and the relationships between the extent of drug binding and desialylation and the genetic variants of hAGP were examined. The photolabeling specificity of [3H]FNZP was confirmed by findings in which other hAGP-binding ligands inhibited the formation of covalent bonds between [3H]FNZP and hAGP. The photolabeling of asialo-hAGP suggested that sialic acid does not involve in the binding of [3H]FNZP. No difference in the labeling could be found between the F1*S variants and A variant. Similarly, FNZP did not show a difference in binding affinity to the two genetic variants of hAGP. Sequence analysis of the photolabeled peptide indicated a sequence corresponding to Tyr91-Arg105 of hAGP.
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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:month |
Oct
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pubmed:issn |
0006-3002
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
10
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pubmed:volume |
1725
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
385-93
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pubmed:dateRevised |
2008-11-21
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pubmed:meshHeading |
pubmed-meshheading:15978731-Amino Acid Sequence,
pubmed-meshheading:15978731-Asialoglycoproteins,
pubmed-meshheading:15978731-Binding Sites,
pubmed-meshheading:15978731-Cyanogen Bromide,
pubmed-meshheading:15978731-Flunitrazepam,
pubmed-meshheading:15978731-Genetic Variation,
pubmed-meshheading:15978731-Humans,
pubmed-meshheading:15978731-Molecular Sequence Data,
pubmed-meshheading:15978731-Orosomucoid,
pubmed-meshheading:15978731-Peptide Fragments,
pubmed-meshheading:15978731-Photoaffinity Labels,
pubmed-meshheading:15978731-Trypsin
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pubmed:year |
2005
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pubmed:articleTitle |
Characterization of benzodiazepine binding site on human alpha1-acid glycoprotein using flunitrazepam as a photolabeling agent.
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pubmed:affiliation |
Department of Biopharmaceutics, Graduate School of Pharmaceutical Sciences, Kumamoto University, 5-1 Oe-honmachi, Kumamoto, 862-0973, Japan.
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pubmed:publicationType |
Journal Article
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