作者: D M Tollefsen , M E Peacock , W J Monafo
DOI: 10.1016/S0021-9258(19)84460-5
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摘要: Heparin cofactor II (HCII) inhibits thrombin rapidly in human plasma the presence of heparin or dermatan sulfate. To determine minimum structure sulfate required to activate HCII, glycosaminoglycan was partially degraded by sequential treatment with periodate, [3H]borohydride, and sulfuric acid. Labeled oligosaccharide fragments were separated gel filtration chromatography. Purified then applied a column HCII bound concanavalin A-Sepharose, oligosaccharides eluted gradient sodium chloride. Di-, tetra-, hexasaccharide did not bind while 15% octasaccharides up 45% larger bound. Octasaccharides that had greater negative charge than run-through material based on anion-exchange chromatography, suggesting they contained number groups per molecule. Fragments containing 12-14 sugar residues accelerated inhibition HCII. this length immobilized molar specific activities those bind. These studies suggest is activated equal 12 contain octasaccharide sequence for binding inhibitor.