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Received June 1, 2007
Accepted March 30, 2008
articles This is an Open-Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/bync/3.0) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Protein binding study of catechin hydrate and genistein by high-performance frontal analysis

Center for Advanced Bioseperation Technology, Department of Chemical Engineering, Inha University, Incheon 402-751, Korea
rowkho@inha.ac.kr
Korean Journal of Chemical Engineering, November 2008, 25(6), 1473-1476(4), 10.1007/s11814-008-0242-8
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Abstract

High-performance frontal analysis (HPFA) was used for the protein binding study of catechin hydrate and genistein to human serum albumin (HSA). The experiment was performed on a Develosil 100Diol-5 column, and sodium phosphate buffer (pH 7.4 and ionic strength of 0.17) was used as the mobile phase. The mixtures of the drug-HSA solution were directly injected into the HPFA column, the HSA was eluted first and the unbound drugs were eluted out as a trapezoidal peak with a plateau region. The unbound drug concentration was determined from a plateau height of the plateau region and the experimental data were fitted by Scatchard equation. The binding constants (K) and binding affinities (nK) of the drug to HAS were K=1.32×10^(4) (L mol^(-1)), nK=0.47×10^(4) (L mol^(-1)) for catechin hydrate, and K=5.17×10^(4) (L mol^(-1)), nK=2.14×10^(4) (L mol^(-1)) for genistein.

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