Isolation and characterization of proteoglycan derived from human placentaand its biological activities

Chondroitin sulfates proteoglycans were isolated from human placenta. For t he identification of enzymatic digestion products of isolated proteoglycan, strong anion exchange-high was pe;formed. By the action of chondroitin per formance liquid chromatography (SAX-HPLC) ABC and chondroitin B lyase, thre e unsaturated disaccharides 2-acetamide-2-deoxy-3-O-(beta-D-gluco-4-enepyra nosyluronic acid)-D-galactose (Delta Di-OS), 2-acetamide-2-deoxy-3-O-(beta- D-gluco-4-enepyranosyluronic acid)-6-O-sulfo-D-galactose (Delta Di-6S) and 2-acetamide-2-deoxy-3-O-(beta-D-gluco-4-enepyranoxyluronic acid)-4-O-sulfo- D-galactose (Delta Di-4S) were produced from the human placenta proteoglyca n. The anticoagulant activity of chondroitin sulfate proteoglycan was evalu ated by activated partial thromboplastin time (aPTT) assay and thrombin tim e (TT) assay. The dotting times of aPTT and TT were increased from 72 to 14 4 sec and 19 to 27 sec, respectively The immune-modulating activity of chon droitin sulfate proteoglycan was examined by cell proliferation assay and t hese results suggest that it may play a role in suppression of the function of immune-related cells.