Skip to main content

Intein-Mediated Expression and Purification of an Analog of Glucagon-like Peptide-1 in Escherichia coli

Buy Article:

$63.00 plus tax (Refund Policy)

Abstract:

To facilitate expression and purification of an analog of GLP-1 (mGLP-1), an intein system was employed in this study. A recombinant fusion protein, CBD-DnaB-mGLP-1, was constructed and expressed in the form of inclusion body. After refolding, the intein-mediated self-cleavage was triggered by pH and temperature shift. By using chitin beads column followed by single step purification, about 2.58 mg of mGLP-1 with the purity of up to 98% could be obtained from 1 L medium. Tricine-SDS-PAGE, RP-HPLC, and ESI-MS were undertaken to determine the purity and molecular weight of mGLP-1. The glucose-lowering activity of mGLP-1 was also preliminarily determined.





Keywords: Chitin beads; expression and purification; glucagon-like peptide-1; incretin; intein; self-cleavage

Document Type: Research Article

Publication date: 2010-10-01

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
X
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more