Next Article in Journal
Genetic Exchange of Multidrug Efflux Pumps among Two Enterobacterial Species with Distinctive Ecological Niches
Next Article in Special Issue
Effect of Nanoparticles on Protein Folding and Fibrillogenesis
Previous Article in Journal
Biodegradable Polydepsipeptides
Previous Article in Special Issue
Folding, Stability and Shape of Proteins in Crowded Environments: Experimental and Computational Approaches
Article Menu

Export Article

Open AccessArticle
Int. J. Mol. Sci. 2009, 10(2), 616-628; doi:10.3390/ijms10020616

A New Approach for Characterizing the Intermediate Feature of α-Chymotrypsin Refolding by Hydrophobic Interaction Chromatography

1
Institute of Modern Separation Science, Shaanxi Key Laboratory of Modern Separation Science, Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, Northwest University, 710069 Xi’an, P.R. China
2
Xinxiang Medical College, Xinxiang, 453003, Henan Province, P.R. China
*
Author to whom correspondence should be addressed.
Received: 31 October 2008 / Revised: 15 February 2009 / Accepted: 17 February 2009 / Published: 18 February 2009
(This article belongs to the Special Issue Protein Folding 2009)
View Full-Text   |   Download PDF [288 KB, uploaded 19 June 2014]   |  

Abstract

A new approach for characterizing the intermediate of urea-denatured α-chymotrypsin (α-Chy) by hydrophobic interaction chromatography (HIC) is presented. The contact surface region (Z, S), affinity (logI), and the character of interaction force (j) of the α-Chy to the stationary phase of HIC (STHIC) between the intermediate (M) and native (N) states were found to be quite different as urea concentration (Curea) changes. With the changes in Curea, a linear relationship between logI and Z was found to exist only for its N state, not for M state, indicating the interaction force between α-Chy in N state to the STHIC to be non-selective, but selective one for its M state. Also, the measured magnitude of both logI and Z in M state is only a fifth of that in N state. All three parameters were employed to distinguish protein in the N state from that in the M state. It would be expected that this result could be employed to distinguish any kind of non-functional protein having correct three-, or four-dimensional molecular structure from their stable M state of any kinds of proteins, and/or other proteins in proteome investigation, separation process of protein, and intensively understanding the intrinsic rule of protein folding in molecular biology.
Keywords: Protein folding; protein drugs; misfolding; intermediates; protein folding liquid chromatography; characterization; hydrophobic interaction chromatography; α-Chymotrypsin; stoichiometric displacement theory Protein folding; protein drugs; misfolding; intermediates; protein folding liquid chromatography; characterization; hydrophobic interaction chromatography; α-Chymotrypsin; stoichiometric displacement theory
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Ke, C.; Li, J.; Liu, Z.; Geng, X. A New Approach for Characterizing the Intermediate Feature of α-Chymotrypsin Refolding by Hydrophobic Interaction Chromatography. Int. J. Mol. Sci. 2009, 10, 616-628.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top