Table of Contents
ISRN Analytical Chemistry
Volume 2013, Article ID 391053, 5 pages
Research Article

Determination of the Binding Parameters between Proteins and Luminol by Chemiluminescence Using Flow Injection Technique

Key Laboratory of Synthetic and Natural Functional Molecule Chemistry of Ministry of Education, College of Chemistry & Material Science, Northwest University, Xi'an 710069, China

Received 8 April 2013; Accepted 16 May 2013

Academic Editors: Z. Arslan and K. Ohyama

Copyright © 2013 Jie Guo et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The interaction behavior of bovine serum albumin (BSA), lysozyme (LYS), myoglobin (MB), and catalase (CAT) with luminol, respectively, was first studied by chemiluminescence (CL) using flow injection (FI) technique based on the fact that the studied proteins can enhance the CL intensity of luminol. A FI-CL model of protein-luminol interaction, , was constructed, and the interaction parameters of BSA, LYS, MB, and CAT with luminol were determined accordingly. The binding constants are in the descending order of CAT > MB > LYS > BSA at the level of 105 to 107 L mol−1, and the number of binding sites of luminol to BSA or LYS is around 2 and to MB or CAT is around 1. The results of thermodynamic parameters (, , and ) showed that the binding processes of luminol to the four proteins are spontaneous mainly through the hydrophobic force.