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Journal of Biomedicine and Biotechnology
Volume 2009, Article ID 104094, 9 pages
http://dx.doi.org/10.1155/2009/104094
Research Article

Characterization for Binding Complex Formation with Site-Directly Immobilized Antibodies Enhancing Detection Capability of Cardiac Troponin I

1Program for Bio-Microsystem Technology, Korea University, 1, 5-ka, Anam-dong, Sungbuk-ku, Seoul 136-701, South Korea
2Department of Biotechnology and Bioinformatics, Korea University, Jochiwon, Choongnam 339-800, South Korea

Received 13 May 2009; Accepted 14 July 2009

Academic Editor: Hicham Fenniri

Copyright © 2009 Il-Hoon Cho 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.

Abstract

The enhanced analytical performances of immunoassays that employed site-directly immobilized antibodies as the capture binders have been functionally characterized in terms of antigen-antibody complex formation on solid surfaces. Three antibody species specific to cardiac troponin I, immunoglobulin G (IgG), Fab, and F were site-directly biotinylated within the hinge region and then immobilized via a streptavidin-biotin linkage. The new binders were more efficient capture antibodies in the immunoassays compared to randomly bound IgG, particularly, in the low antibody density range. The observed improvements could have resulted from controlled molecular orientation and also from flexibility, offering conditions suitable for binding complex formations.