What is he best known for?
The fields of study he is best known for:
- Enzyme
- Biochemistry
- Chromatography
David S. Hage mostly deals with Chromatography, Affinity chromatography, Human serum albumin, Elution and Plasma protein binding.
His study in Enantiomer extends to Chromatography with its themes.
His Affinity chromatography study integrates concerns from other disciplines, such as Stationary phase, Albumin and Adsorption.
His Human serum albumin research includes themes of Ionic strength, Allosteric regulation and Serum albumin.
The various areas that David S. Hage examines in his Serum albumin study include Binding site and Ligand.
His Plasma protein binding research integrates issues from Blood proteins, Protein ligand, Proton NMR and Drug.
His most cited work include:
- Affinity Chromatography: A Review of Clinical Applications (198 citations)
- Affinity monolith chromatography. (186 citations)
- Review: Glycation of human serum albumin (185 citations)
What are the main themes of his work throughout his whole career to date?
The scientist’s investigation covers issues in Chromatography, Affinity chromatography, Human serum albumin, Plasma protein binding and Elution.
His Chromatography research is multidisciplinary, incorporating elements of Equilibrium constant and Binding site.
His study in Affinity chromatography is interdisciplinary in nature, drawing from both Albumin, Enantiomer, Stationary phase and Drug.
His Human serum albumin research is multidisciplinary, relying on both Sulfonylurea, Glycation, Blood proteins and Serum albumin.
His Serum albumin research is multidisciplinary, incorporating perspectives in Stereochemistry and Acetohexamide.
David S. Hage interconnects Orosomucoid and Glycoprotein in the investigation of issues within Plasma protein binding.
He most often published in these fields:
- Chromatography (80.07%)
- Affinity chromatography (47.83%)
- Human serum albumin (38.77%)
What were the highlights of his more recent work (between 2015-2021)?
- Chromatography (80.07%)
- Affinity chromatography (47.83%)
- Human serum albumin (38.77%)
In recent papers he was focusing on the following fields of study:
Chromatography, Affinity chromatography, Human serum albumin, Plasma protein binding and Elution are his primary areas of study.
The concepts of his Chromatography study are interwoven with issues in Orosomucoid, Glycoprotein and Drug.
His Affinity chromatography study combines topics in areas such as Blood proteins, Analyte and Stationary phase.
His biological study spans a wide range of topics, including Sulfonylurea, Glycation, High-performance liquid chromatography and Protein G.
His Plasma protein binding research focuses on subjects like Equilibrium constant, which are linked to Fraction, Quantitative analysis, Acetohexamide and Tolbutamide.
His work carried out in the field of Elution brings together such families of science as Concanavalin A and Fucosylation.
Between 2015 and 2021, his most popular works were:
- Dual-Target Binding Ligands with Modulated Pharmacokinetics for Endoradiotherapy of Prostate Cancer. (32 citations)
- High performance affinity chromatography and related separation methods for the analysis of biological and pharmaceutical agents (26 citations)
- Affinity monolith chromatography: A review of general principles and applications. (24 citations)
In his most recent research, the most cited papers focused on:
- Enzyme
- Biochemistry
- Organic chemistry
His primary areas of investigation include Chromatography, Affinity chromatography, Plasma protein binding, Elution and Human serum albumin.
His biological study focuses on Hydrophilic interaction chromatography.
David S. Hage has researched Affinity chromatography in several fields, including Separation method, Analyte and Flexibility.
David S. Hage combines subjects such as Stationary phase and Agarose with his study of Analyte.
His study looks at the intersection of Plasma protein binding and topics like Blood proteins with Ultrafiltration.
The study incorporates disciplines such as Allosteric regulation, Solvent and Protein–protein interaction in addition to Elution.
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