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Related Concept Videos

Affinity Chromatography01:03

Affinity Chromatography

Affinity chromatography is a powerful technique extensively utilized for separating and purifying specific biomolecules from complex mixtures. It capitalizes on the highly selective binding between an analyte and its counterpart, such as antibody-antigen interactions. The counterpart is immobilized on the stationary phase, forming an affinity column. The stationary phase typically consists of solid support, such as agarose or porous glass beads, immobilizing the affinity ligand. The mobile...

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Related Experiment Video

Updated: May 22, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

Search for amyloid-binding proteins by affinity chromatography.

Miguel Calero1, Agueda Rostagno, Jorge Ghiso

  • 1Centro Nacional de Microbiología, Instituto de Salud Carlos III, Majadahonda, Madrid, Spain. mcalero@isciii.es

Methods in Molecular Biology (Clifton, N.J.)
|April 25, 2012
PubMed
Summary

Researchers identified key proteins that bind to amyloid peptides, which could impact their function and disease relevance. This study developed a method to isolate and characterize these amyloid-binding proteins from human plasma.

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Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
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Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

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Last Updated: May 22, 2026

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease
15:23

Selection of Aptamers for Amyloid β-Protein, the Causative Agent of Alzheimer's Disease

Published on: May 13, 2010

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis
10:03

Screening for Amyloid Aggregation by Semi-Denaturing Detergent-Agarose Gel Electrophoresis

Published on: July 16, 2008

Area of Science:

  • Biochemistry
  • Proteomics
  • Neuroscience

Background:

  • Amyloid-binding proteins influence the physiological and pathological roles of amyloidogenic peptides and proteins.
  • Understanding these interactions is crucial for modulating amyloid functions, including solubility, transport, clearance, degradation, and fibril formation.

Purpose of the Study:

  • To develop and demonstrate a simple affinity chromatography protocol for isolating and characterizing amyloid-binding proteins.
  • To identify specific amyloid-binding proteins in human plasma, with a focus on those interacting with Alzheimer's amyloid-beta (Aβ) peptides.

Main Methods:

  • Affinity chromatography utilizing sequential elution steps to isolate proteins based on their binding interactions.
  • Biochemical analysis of eluted proteins to identify their identity and binding characteristics.

Main Results:

  • The protocol successfully isolated and identified amyloid-binding proteins from human plasma.
  • Serum amyloid P component (SAP) and apolipoprotein J (clusterin) were identified as major Aβ-binding proteins.
  • Minor Aβ-binding proteins included various apolipoproteins (apoA-IV, apoE, apoA-I), albumin (HSA), and fibulin.

Conclusions:

  • The developed affinity chromatography method is effective for characterizing amyloid-binding proteins.
  • SAP and clusterin are significant plasma proteins involved in binding Aβ, potentially influencing Alzheimer's disease pathology.
  • Further research can utilize this method to explore other amyloid-protein interactions and their implications.