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Cloning and expression of a novel insulin-releasing peptide, brevinin-2GU from Escherichia coli

Paper ID Volume ID Publish Year Pages File Format Full-Text
21342 43217 2009 4 PDF Available
Title
Cloning and expression of a novel insulin-releasing peptide, brevinin-2GU from Escherichia coli
Abstract

Brevinin-2GU, a member of a brevinin-2 family of antimicrobial peptides isolated from an extract of the skin of the Asian frog, Hylarana guntheri, displays significant insulin-releasing activity. In this study, in order to obtain relatively large quantity of functional brevinin-2GU protein, the coding sequence of brevinin-2GU gene was cloned into pET32a (+) vector and expression as a Trx fusion protein in Escherichia coli. The results indicated that the expression level of the fusion protein could reach up to 45% of the total cell proteins. the soluble fusion protein collected from the supernatant of the cell lysate was then separated by Ni2+-chelating chromatography and cleaved by Factor Xa protease to release mature brevinin-2GU. Our results showed that the final yield of the brevinin-2GU was 1.7 mg, the purified peptide displayed insulin-releasing activity similar to that of the purified brevinin that was reported earlier. This method allows production of sufficiently large amounts of brevinin-2GU peptide for functional and structural characterizations.

Keywords
Brevinin-2GU; Escherichia coli; Expression, Frog skin; Insulin secretion
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Cloning and expression of a novel insulin-releasing peptide, brevinin-2GU from Escherichia coli
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Publisher
Database: Elsevier - ScienceDirect
Journal: Journal of Bioscience and Bioengineering - Volume 107, Issue 4, April 2009, Pages 460–463
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Bioengineering
Get Full-Text Now
Don't Miss Today's Special Offer
Price was $35.95
You save - $31
Price after discount Only $4.95
100% Money Back Guarantee
Full-text PDF Download
Online Support
Any Questions? feel free to contact us