Title : The distinct roles that Gln-192 and Glu-217 of factor IX play in selectivity for macromolecular substrates and inhibitors.

Pub. Date : 2001 Sep 18

PMID : 11551226






4 Functional Relationships(s)
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1 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
2 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
3 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
4 Although all variants formed an SDS-stable complex with antithrombin III (ATIII) equally well in the presence of heparin and were readily inhibited by ATIII in the absence of heparin, activated IXQ192K exhibited a slower stable complex formation with ATIII without heparin. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens