Andersson L O, Hoffman J, Holmer E, Larm O, Larsson K, Söderström G
Thromb Res. 1982 Dec 15;28(6):741-7. doi: 10.1016/0049-3848(82)90099-8.
The anticoagulant activity of a partially reduced sulphated alginic acid, a partially reduced aminated and sulphated alginic acid and sulphated guaran have been studied. The anticoagulant activities in the APTT assay were 28, 39 and 70 IU/mg respectively. None showed any activity in anti-factor Xa assay. Studies on binding to Antithrombin III - Sepharose showed that sulphated guaran and a fraction of the aminated and sulphated alginic acid was bound, whereas no binding occurred with sulphated alginic acid. The inhibition of thrombin activity by these polysaccharides was studied in purified systems with or without added Antithrombin III, using both fibrinogen clotting and chromogenic peptide substrate assays. The two alginic acid preparations showed Antithrombin III-dependent inhibition of thrombin, whereas the sulphated guaran inhibits both by Antithrombin III-dependent and independent mechanisms.
对部分还原的硫酸化海藻酸、部分还原的胺化硫酸化海藻酸和硫酸化瓜尔胶的抗凝血活性进行了研究。在活化部分凝血活酶时间（APTT）测定中的抗凝血活性分别为28、39和70国际单位/毫克。在抗Xa因子测定中均未显示任何活性。与抗凝血酶III - 琼脂糖结合的研究表明，硫酸化瓜尔胶和部分胺化硫酸化海藻酸有结合，而硫酸化海藻酸未发生结合。使用纤维蛋白原凝血和生色肽底物测定法，在添加或不添加抗凝血酶III的纯化系统中研究了这些多糖对凝血酶活性的抑制作用。两种海藻酸制剂显示出抗凝血酶III依赖性的凝血酶抑制作用，而硫酸化瓜尔胶则通过抗凝血酶III依赖性和非依赖性机制发挥抑制作用。
