Abstract
To investigate the processing of transforming growth factor β1 (TGFβ1) pro-protein by furin protease we expressed a GST-pro-TGFβ1 fusion protein in bacteria. Analysis of the furin digestion pattern revealed the liberation of 12.5 kDa TGFβ1 monomers. There was no evidence for cleavage of an alternative furin site within the pro-protein.
Keywords: Transforming growth factor β1, furin, proteolytic processing
Protein & Peptide Letters
Title: Furin Cleavage of Bacterial Expressed Glutathione-S-Transferase-Pro-Transforming Growth Factor β1 Fusion Protein In Vitro
Volume: 17 Issue: 4
Author(s): N. A. Kahle, C. Joffroy, S. L. Popp, C. Knabbe and M. B. Stope
Affiliation:
Keywords: Transforming growth factor β1, furin, proteolytic processing
Abstract: To investigate the processing of transforming growth factor β1 (TGFβ1) pro-protein by furin protease we expressed a GST-pro-TGFβ1 fusion protein in bacteria. Analysis of the furin digestion pattern revealed the liberation of 12.5 kDa TGFβ1 monomers. There was no evidence for cleavage of an alternative furin site within the pro-protein.
Export Options
About this article
Cite this article as:
Kahle A. N., Joffroy C., Popp L. S., Knabbe C. and Stope B. M., Furin Cleavage of Bacterial Expressed Glutathione-S-Transferase-Pro-Transforming Growth Factor β1 Fusion Protein In Vitro, Protein & Peptide Letters 2010; 17 (4) . https://dx.doi.org/10.2174/092986610790963609
DOI https://dx.doi.org/10.2174/092986610790963609 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |
- Author Guidelines
- Graphical Abstracts
- Fabricating and Stating False Information
- Research Misconduct
- Post Publication Discussions and Corrections
- Publishing Ethics and Rectitude
- Increase Visibility of Your Article
- Archiving Policies
- Peer Review Workflow
- Order Your Article Before Print
- Promote Your Article
- Manuscript Transfer Facility
- Editorial Policies
- Allegations from Whistleblowers