Archives of Pharmacal Research

The Pharmaceutical Society of Korea (대한약학회)
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Isolation and Characterization of Proteoglycan Derived From Human Placenta and its Biological Activities

  • Lee, Kyung-Bok (Department of Biochemistry, College of Medicine, Konyang University) ;
  • Kim, Jong-Sig (Department of Chemistry, Konyang University) ;
  • Yoo, Yung-Choon (Department of Microbiology, College of Medicine, Konyang University) ;
  • Kwak, Sang-Tae (Department of Biochemistry, College of Medicine, Konyang University) ;
  • Song, Kyung-Sik (Department of Agricultural Chemistry, College of Agriculture, Kyungpook National University) ;
  • Kim, Yeong-Shik (Natural Products Research Institute, Seoul National University)
  • Published : 2000.04.01
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Abstract

Chondroitin sulfates proteoglycans were isolated from human placenta. For the identification of enzymatic digestion products of isolated proteoglycan, strong anion exchange-high performance liquid chromatography (SAX-HPLC) was performed. By the action of chondroitin ABC and chondroitin B lyase, three unsaturated disaccharides 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-D-galactose ($\delta$Di-OS), 2-acetamide-2-deoxy-3-O-($\beta$-D-gluco-4-enepyranosyluronic acid)-6-O-su lfo-D-galactose ($\delta$Di-6S) and 2-acetamide-2-deoxy-3-O-($\beta$-D-gl uco-4-enepyranosyluronic acid)-4-O-sulfo-D-galactose ($\delta$Di-4S) were produced from the human placenta proteoglycan. The anticoagulant activity of chondroitin sulfate proteoglycan was evaluated by activated partial thromboplastin time (aPTT) assay and thrombin time (TT) assay. The clotting times of aPTT and TT were increased from 72 to 144 sec and 19 to 27 sec, respectively. The Immune-modulating activity of chondroitin sulfate proteoglycan was examined by cell proliferation assay and these results suggest that it may play a role in suppression of the function of immune-related cells.

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