Generic placeholder image

Protein & Peptide Letters

Editor-in-Chief

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

Spectroscopic Studies on Erythrina lysistemon Seed Lectin Effect of Denaturing Agents on Lectin Quaternary Structure

Author(s): Emadeldin H. E. Konozy, Maha B. Dafalla and Chwan-Deng Hsiao

Volume 13, Issue 6, 2006

Page: [581 - 586] Pages: 6

DOI: 10.2174/092986606777145751

Price: $65

Abstract

The equilibrium unfolding of ElysL, a homodimeric legume lectin, was studied using different denaturing agents such as guanidinium chloride (GdnHCl), temperature and pH. Simultaneously, changes in the secondary as well as tertiary structure of lectin were followed by CD spectroscopy examination in both far and near-UV region, respectively. The hydrophobic cluster binding dye, 1-anilino-8-naphthalene sulfonate (ANS), was used to further explore intermediates and to follow the unfolding pathway of lectin. The adenine binding ability of lectin was examined and monitored via absorption spectra and the intrinsic tryptophan fluorescence. Our findings indicate that the ElysL unfolding process occurs via a three state pathway with an intermediate state. We also showed that ElysL binds adenine in a manner that involves a hydrophobic binding pocket that is independent of the carbohydrate binding sites.

Keywords: lectin, unfolding, intermediate, Circular dichroism, fluorescence, adenine binding


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