ArticleAnalytical chemistry2015
Analysis of Hormone-Protein Binding in Solution by Ultrafast Affinity Extraction: Interactions of Testosterone with Human Serum Albumin and Sex Hormone Binding Globulin.
Article in Analytical chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 32 citations in OpenAlex.
- Binding of Steroid Hormones to the FA1 and FA6 Sites of Human Serum Albumin through Computational Biology and Quantum Biochemistry.ACS omega · 2026Article
- Microscale Affinity Chromatography for Biointeraction Analysis: Strategies, Principles and Applications.Journal of separation science · 2026Review
- Studies and analysis of drug-target interactions by affinity chromatography and related techniques: A review.Journal of pharmaceutical analysis · 2026Review
- Understanding the Secular Decline in Testosterone: Mechanisms, Consequences, and Clinical Perspectives.International journal of molecular sciences · 2026Review
- Role of noncoding RNA as a pacemaker in cancer stem cell regulation: a review article.Journal of the Egyptian National Cancer Institute · 2025Review
- Analysis of the binding of warfarin to glyoxal- and methylglyoxal-modified human serum albumin by ultrafast affinity extraction.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2022Article
- Evaluation of microcolumn stability in ultrafast affinity extraction for binding and rate studies.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2021Article
- [Advances in chromatography in the study of drug-plasma protein interactions].Se pu = Chinese journal of chromatography · 2021Review
- Characterization of drug binding with alphaJournal of chromatography. A · 2021Article
- Recent Advances in Supramolecular Affinity Separations: Affinity Chromatography and Related Methods.Advances in chromatography · 2021Article
- Affinity chromatography: A review of trends and developments over the past 50 years.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2020Review
- Testosterone meets albumin - the molecular mechanism of sex hormone transport by serum albumins.Chemical science · 2019Article
- Kinetic Analysis by Affinity Chromatography.Frontiers in chemistry · 2019Review
- Binding studies based on ultrafast affinity extraction and single- or two-column systems: Interactions of second- and third-generation sulfonylurea drugs with normal or glycated human serum albumin.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2018Article
- Characterization of solution-phase drug-protein interactions by ultrafast affinity extraction.Methods (San Diego, Calif.) · 2018Article
- High performance affinity chromatography and related separation methods for the analysis of biological and pharmaceutical agents.The Analyst · 2018Review
- Analysis of stereoselective drug interactions with serum proteins by high-performance affinity chromatography: A historical perspective.Journal of pharmaceutical and biomedical analysis · 2017Review
- Chromatographic studies of drug interactions with alphaJournal of chromatography. A · 2017Article
- Analysis of free drug fractions in serum by ultrafast affinity extraction and two-dimensional affinity chromatography using α1-acid glycoprotein microcolumns.Journal of chromatography. A · 2016Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Ultrafast affinity extraction was used to study hormone-protein interactions in solution, using testosterone and its transport proteins human serum albumin (HSA) and sex hormone binding globulin (SHBG) as models. Both single column and two-dimensional systems based on HSA microcolumns were utilized to measure the free fraction of testosterone in hormone/protein mixtures at equilibrium or that were allowed to dissociate for various lengths of time. These data were used to determine the association equilibrium constants (Ka) or global affinities (nKa') and dissociation rate constants (kd) for testosterone with soluble HSA and SHBG. This method was also used to measure simultaneously the free fraction of testosterone and its equilibrium constants with both these proteins in physiological mixtures of these agents. The kd and Ka values obtained for HSA were 2.1-2.2 s(-1) and 3.2-3.5 × 10(4) M(-1) at pH 7.4 and 37 °C. The corresponding constants for SHBG were 0.053-0.058 s(-1) and 0.7-1.2 × 10(9) M(-1). All of these results gave good agreement with literature values, indicating that this approach could provide information on a wide range of rate constants and binding strengths for hormone-protein interactions in solution and at clinically relevant concentrations. The same method could be extended to alternative hormone-protein systems or other solutes and binding agents.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.