Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10801018 | Biochimica et Biophysica Acta (BBA) - General Subjects | 2005 | 9 Pages |
Abstract
The binding of flunitrazepam (FNZP) by human α1-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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Authors
Victor Tuan Giam Chuang, Motoki Hijioka, Masaaki Katsuki, Koji Nishi, Teppei Hara, Ken-ichi Kaneko, Megumi Ueno, Akihiko Kuniyasu, Hitoshi Nakayama, Masaki Otagiri,