Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Evidence for differences in the binding of drugs to the two main genetic variants of human alpha 1-acid glycoprotein.

British journal of clinical pharmacology - 1 Sept 1993

Herve F, Gomas E, Duche J C, Tillement J P

Abstract excerpt

1. Human alpha 1-acid glycoprotein (AAG), a plasma transport protein, has three main genetic variants. F1. S and A. Native commercial AAG (a mixture of almost equal proportions of these three variants) has been separated by chromatography into variants which correspond to the proteins of the two genes which code for AAG in humans: the A variant and a mixture of the F1 and S variants (60% F1 and 40% S). Their...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Genetic Variation
Share to In Vitro Techniques
Share to Orosomucoid

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Protein Binding

Source

Open in PubMed Open full text

Identifiers

PMID: 9114911
DOI: 10.1111/j.1365-2125.1993.tb04224.x
PMCID: PMC1364645

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Evidence for differences in the binding of drugs to the two main genetic variants of human alpha 1-acid glycoprotein.PMID 9114911Read ↗

Binding of disopyramide, methadone, dipyridamole, chlorpromazine, lignocaine and progesterone to the two main genetic variants of human alpha 1-acid glycoprotein: evidence for drug-binding differences between the variants and for the presence of two separate drug-binding sites on alpha 1-acid glycoprotein.Semantic proximity Read ↗

The genetic variant A of human alpha 1-acid glycoprotein limits the blood to brain transfer of drugs it binds.Semantic proximity Read ↗

Lipophilicity Influences Drug Binding to α1-Acid Glycoprotein F1/S Variants But Not to the A Variant.Semantic proximity Read ↗

Ligand specificity of the genetic variants of human alpha1-acid glycoprotein: generation of a three-dimensional quantitative structure-activity relationship model for drug binding to the A variant.Semantic proximity Read ↗

Two-step chromatographic purification of human plasma alpha(1)-acid glycoprotein: its application to the purification of rare phenotype samples of the protein and their study by chromatography on immobilized metal chelate affinity adsorbent.Semantic proximity Read ↗

Selective binding of tamsulosin to genetic variants of human alpha1-acid glycoprotein.Semantic proximity Read ↗

Evaluation of selective competitive binding of basic drugs to alpha1-acid glycoprotein variants.Semantic proximity Read ↗

One step purification of alpha(1)-acid glycoprotein from human plasma. Fractionation of its polymorphic allele products.Semantic proximity Read ↗

Selective binding of coumarin enantiomers to human alpha1-acid glycoprotein genetic variants.Semantic proximity Read ↗

Selective binding interactions of deramciclane to the genetic variants of human alpha(1)-acid glycoprotein.Semantic proximity Read ↗

Binding of d-methadone, l-methadone, and dl-methadone to proteins in plasma of healthy volunteers: role of the variants of alpha 1-acid glycoprotein.Semantic proximity Read ↗

A site-directed mutagenesis study of drug-binding selectivity in genetic variants of human alpha(1)-acid glycoprotein.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.