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The paper describes the activation mode and the glycosic linkage of anti-complementary polysaccharide isolated from Cinnamomum cassia. The polysaccharide fractions, CC-Ⅲa, CC-Ⅲb, and CC-Ⅲc, activated C3 component existed in normal human serum and produced C3 cleavage segments, C3a and C3b. The polysaccharide, CC-2-Ⅲa-3 activated the complement system both in the presence and absence of Ca^(++), suggesting that it involved in both classical and alternative complement path￢ways. Methylation of CC-2-Ⅲa-3 was performed with methylsulphinyl carbanion and methyl iodide in DMSO. The methylated products was hydrolyzed, then converted into the partially methylated alditol acetates. Gas chromatography-mass spectrometry(GC-MS) revealed derivatives of terminal Glcρ and Galρ, l,2-linked Rhaρ, 1,6-linked Manρ, l,3-linked Glcρ, 1,6-linked Galρ etc.
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