Modification of Arabinogalactan Isolated from Larix sibirica Ledeb. into Sulfated Derivatives with the Controlled Molecular Weights.

The process of sulfation of arabinogalactan-a natural polysaccharide from Larix sibirica Ledeb.-with sulfamic acid in 1,4-dioxane using different activators has been studied for the first time. The dynamics of the molecular weight of sulfated arabinogalactan upon variation in the temperature and time of sulfation of arabinogalactan with sulfamic acid in 1,4-dioxane has been investigated. It has been found that, as the sulfation time increases from 10 to 90 min, the molecular weights of the reaction products grow due to the introduction of sulfate groups without significant destruction of the initial polymer and sulfation products. Sulfation at 95 °C for 20 min yields the products with a higher molecular weight than in the case of sulfation at 85 °C, which is related to an increase in the sulfation rate; however, during the further process occurring under these conditions, sulfation is accompanied by the destruction and the molecular weight of the sulfated polymer decreases. The numerical optimization of arabinogalactan sulfation process has been performed. It has been shown that the optimal parameters for obtaining a product with a high sulfur content are a sulfamic acid amount of 20 mmol per 1 g of arabinogalactan, a process temperature of 85 °C, and a process time of 2.5 h.

Anticoagulant-active sulfated arabinogalactan from Chaetomorpha linum: Structural characterization and action on coagulation factors.

A sulfated polysaccharide from the green alga Chaetomorpha linum, designated CLS4, was isolated by water extraction, anion-exchange and size-exclusion chromatography. Chemical and spectroscopic analyses demonstrated that CLS4 was a sulfated arabinogalactan, which was constituted by (1→6)-ß-d-galactopyranose and (1→5)-α-l-arabinofuranose residues with sulfate groups at C-2/ C-3 of (1→5)-α-l-arabinofuranose and C-2/C-4 of (1→6)-ß-d-galactopyranose. CLS4 possessed strong anticoagulant activity in vitro or in vivo as evaluated by activated partial thromboplastin time and thrombin time assays. CLS4 largely inhibited the activities of the coagulation factors XII, XI, IX and VIII. CLS4 was a potent thrombin inhibitor mediated by antithrombin III (ATIII) or heparin cofactor II, and it also effectively stimulated the factor Xa inhibition by potentiating ATIII. Moreover, CLS4 had a high thrombolytic activity in vitro as assessed by clot lytic rate assay. The results suggested that CLS4 could be a promising source of anticoagulant agent.