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Analysis of Protein Folding, Transport, and Degradation in Living Cells by Radioactive Pulse Chase
Published on: February 12, 2019
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Pulse Chase of Suspension Cells
Lai-Yee Wong1, QiMing Liang1, Kevin Brulois1
1Department of Molecular Microbiology and Immunology, University of Southern California, Los Angeles, CA, USA.
Bio-Protocol
|January 13, 2021
Summary
The pulse-chase method tracks protein dynamics using metabolic labeling. This protocol details its use for studying immunoglobulin folding and disulfide bond formation in suspension cells.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- The pulse-chase method is essential for analyzing protein dynamics over time.
- Understanding protein folding and disulfide bond formation is crucial for cellular function.
Purpose of the Study:
- To describe a protocol for studying immunoglobulin folding and disulfide bond formation.
- To adapt the pulse-chase technique for analyzing protein degradation and secretion.
Main Methods:
- Utilizing the pulse-chase technique with metabolic labeling (e.g., radiolabeled amino acids).
- Applying the method to suspension cells for observing protein dynamics.
- Focusing on immunoglobulin folding and disulfide bond formation.
Main Results:
- The protocol provides specific conditions for studying protein folding and disulfide bond formation.
- The method is adaptable for assessing protein degradation rates.
- The method is adaptable for assessing protein secretion.
Conclusions:
- The described pulse-chase protocol is effective for investigating immunoglobulin folding and disulfide bond formation in suspension cells.
- This technique offers a versatile approach for studying various aspects of protein dynamics, including degradation and secretion.
