Title : Interaction of antithrombin with sulfated, low molecular weight lignins: opportunities for potent, selective modulation of antithrombin function.

Pub. Date : 2009 Jul 31

PMID : 19497853






1 Functional Relationships(s)
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1 Salt dependence of binding affinity indicates that the antithrombin-sulfated DHP interaction involves a massive 80-87% non-ionic component to the free energy of binding. Salts serpin family C member 1 Homo sapiens