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Chromatographia

, Volume 70, Issue 3–4, pp 475–479 | Cite as

Affinity CE Determination of the Binding Constant of Bioactive Sulfated Polysaccharide 916 to Human Serum Albumin

  • Zhi Yang
  • Zhi-Hua Lv
  • Ting-Fu Jiang
  • Yuan-Hong Wang
Original

Abstract

Drug-protein binding is an important process in determining the activity of a pharmaceutical agent once it has entered the body. This paper developed an affinity capillary electrophoresis method to determine the binding constant between a bioactive sulfated polysaccharide 916 (916) and a potential protein, human serum albumin. This method is based on the principle that the changing analytes have different mobility shift in the zone electrophoresis. A fixed amount of protein was injected into a capillary filled with a background electrolyte containing the polysaccharide in varying concentrations. The effective mobility data of the protein were processed according to classical linearization treatments to obtain the binding constant of 916 to the HSA complex. The binding constant Ka of 916 to the human serum albumin achieved was 2.1 × 104.

Keywords

Affinity capillary electrophoresis Binding constant Human serum albumin Sulfated polysaccharide 916 

Notes

Acknowledgments

This work was funded by the Chinese High-tech Project “863” (2006AA090401) and an open research fund program of the key laboratory of marine drugs (Ocean University of China), Ministry of Education (KLMD (OUC) 200601).

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Copyright information

© Vieweg+Teubner | GWV Fachverlage GmbH 2009

Authors and Affiliations

  1. 1.School of Medicine and PharmacyOcean University of ChinaQingdaoPeople’s Republic of China

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