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Affinity Chromatography

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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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Updated: Mar 18, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

Published on: December 9, 2016

Protein Complex Purification by Affinity Capture.

John LaCava¹, Javier Fernandez-Martinez¹, Zhanna Hakhverdyan¹

¹Laboratory of Cellular and Structural Biology, The Rockefeller University, New York, New York 10065.

Cold Spring Harbor Protocols

|July 3, 2016

Summary

This summary is machine-generated.

Affinity capture purifies yeast protein complexes for study. This method isolates biological assemblies, enabling deeper interactomic exploration and biochemical analysis.

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Last Updated: Mar 18, 2026

Protein Complex Affinity Capture from Cryomilled Mammalian Cells

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Published on: December 9, 2016

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling

Published on: April 1, 2017

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The MultiBac Protein Complex Production Platform at the EMBL

Published on: July 11, 2013

Area of Science:

Biochemistry
Molecular Biology
Proteomics

Background:

Affinity capture is a key technique for isolating protein complexes.
Studying endogenous protein complexes is crucial for understanding cellular functions.
Previous methods faced challenges in accessing and analyzing these complexes.

Purpose of the Study:

To outline methods for purifying endogenous yeast protein complexes.
To discuss considerations for successful affinity capture strategies.
To facilitate interactomic exploration of yeast proteomes.

Main Methods:

Cell lysis and extraction to release protein complexes.
Enrichment of target complexes using affinity reagents (e.g., antibodies).
Utilizing solid supports coupled with affinity reagents for complex isolation.

Main Results:

Demonstrated the effectiveness of affinity capture for endogenous complex purification.
Enabled subsequent biochemical and biophysical assays on purified complexes.
Facilitated broader exploration of protein interactions within yeast.

Conclusions:

Affinity capture provides a robust approach for studying endogenous protein complexes.
This technique enhances the accessibility of previously intractable biological assemblies.
It is a valuable tool for interactomic research in yeast and other model organisms.