Kb. Lee et al., Isolation and characterization of proteoglycan derived from human placentaand its biological activities, ARCH PH RES, 23(2), 2000, pp. 182-186
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.