Title : The interaction of glycosaminoglycans with heparin cofactor II: structure and activity of a high-affinity dermatan sulfate hexasaccharide.

Pub. Date : 1992

PMID : 1442260






6 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 The binding sites for dermatan sulfate and heparin in HCII overlap but are not identical. Dermatan Sulfate serpin family D member 1 Homo sapiens
2 This may explain the observation that HCII binds non-specifically to heparin oligosaccharides but preferentially binds to a minor hexasaccharide isolated from dermatan sulfate having the structure shown in Fig. Dermatan Sulfate serpin family D member 1 Homo sapiens
3 The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo. Dermatan Sulfate serpin family D member 1 Homo sapiens
4 The tissue distribution of dermatan sulfate molecules containing the high-affinity HCII binding site may regulate HCII activity in vivo. Dermatan Sulfate serpin family D member 1 Homo sapiens
5 Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction. Dermatan Sulfate serpin family D member 1 Homo sapiens
6 Finally, in the presence of dermatan sulfate or heparin, the N-terminal acidic domain of HCII may interact with the hirudin-binding site of thrombin to produce maximal stimulation of the thrombin-HCII reaction. Dermatan Sulfate serpin family D member 1 Homo sapiens