Abstract
Anti-sera against a complement-activating pectin (AR-2IIb), which was purified from
the roots of Angelica acutiloba Kitagawa, were obtained by immunization of rabbits, and a polyclonal anti-AR-2IIb
antibody of the IgG class was purified by affinity chromatography on AR-2IIb-immobilized
Sepharose and Protein G-Sepharose. Periodate oxidation of AR-2IIb significantly reduced
its inhibitory activity on the reactivity of AR-2IIb to anti-AR-2IIb-IgG, but pronase
digestion of AR-2IIb did not affect its inhibitory activity.
Other pharmacologically active pectins from A. autiloba, Bupleurum falcatum, and Glycyrrhiza uralensis and the complement-activating pectic arabinogalactan from A. autiloba also showed significant inhibitory activities on the reactivity of AR-2IIb to anti-AR-2IIb-IgG,
but these inhibitory activities were lower than that of AR-2IIb. Other pectins, polygalacturonic
acid, arabinogalactan, galactan, and araban tested had negligible inhibitory activity.
Endo-α-(1→4)- polygalacturonase digestion of AR-2IIb indicated that its “ramified” region
(rhamnogalacturonan core possessing neutral oligosaccharide side-chains) contained
epitopes for anti-AR-2IIb-IgG, but that 2-keto-3-deoxyoctulosonic acid (KDO)-containing
regions and oligogalacturonides obtained from AR-2IIb were not recognized by anti-AR-2IIb-IgG.
Although carboxyl-reduction of galacturonic acid in the “ramified” region decreased
the inhibitory activity of the “ramified” region on its reactivity to anti-AR-2IIb,
an acidic tetrasaccharide unit in the rhamnogalacturonan core had negligible inhibitory
activity.
Key words
Angelica acutiloba Kitagawa - Apiaceae - complement-activating pectin - anti-pectin antibody