Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

ISSN (Print): 0929-8665
ISSN (Online): 1875-5305

Enhanced Soluble Production of Biologically Active Recombinant Human p38 Mitogen-Activated-Protein Kinase (MAPK) in Escherichia coli

Author(s): Sunil K. Khattar, Pankaj Gulati, Prabuddha K. Kundu, Vibhuti Singh, Usha Bughani, Malini Bajpai and Kulvinder. S. Saini

Volume 14, Issue 8, 2007

Page: [756 - 760] Pages: 5

DOI: 10.2174/092986607781483660

Price: $65

Abstract

The conditions were optimized for maximum soluble yield of biologically active recombinant p38α mitogen activated protein kinase (MAPK) vis-a-vis insoluble fraction (inclusion body formation). This study reports a rapid, economical and single step purification process for the overproduction of GST tagged p38α MAPK. A yield of 18 mg of highly purified and soluble protein per liter of bacterial culture within 6 h timeframe was achieved. The purified protein was found to be biologically suitable for phosphorylation by upstream kinases and was catalytically active. We further demonstrated that our in-house p38α MAPK is more potent ( > 30%) than a commercially available enzyme.

Keywords: Affinity chromatography, enzyme kinetics, GST tag, MKK6, phosphorylation, soluble p38α MAPK


Rights & Permissions Print Cite
© 2024 Bentham Science Publishers | Privacy Policy