Title : Antithrombin-III-Hamilton, Ala 382 to Thr: an antithrombin-III variant that acts as a substrate but not an inhibitor of alpha-thrombin and factor Xa.

Pub. Date : 1991 May 15

PMID : 2029579






5 Functional Relationships(s)
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1 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
2 When AT-III was isolated from the plasma of the propositus by heparin-Sepharose chromatography, it had identical mobility on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to normal plasma-derived AT-III, under both reducing and nonreducing conditions. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
3 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
4 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens
5 However, the AT-III-Hamilton species, separated from the propositus" normal AT-III by a combination of heparin-Sepharose and thrombin-Sepharose chromatography, had increased mobility on reductive SDS-PAGE compared with AT-III from the propositus isolated by heparin-Sepharose chromatography alone. Sodium Dodecyl Sulfate serpin family C member 1 Homo sapiens