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Histidine-rich glycoprotein inhibits contact activation of blood coagulation
A B Vestergaard1, H F Andersen, S Magnusson
1Department of Molecular Biology and Plant Physiology, University of Aarhus, Denmark.
Abstract:
Histidine-rich glycoprotein has been purified from bovine plasma employing two different purification procedures. The first procedure was one-step ion-exchange chromatography using phosphocellulose, while the second procedure involved fractionation using polyethyleneglycol 6000 followed by column chromatography employing CM-Sepharose and heparin-Sepharose. The effect of purified bovine histidine-rich glycoprotein on the contact activation of blood coagulation was studied in human plasma by using as activating surface either an ellagic acid-phospholipid suspension (Cephotest) or sulfatide. Contact activation was monitored by the generation of amidolytic activity towards a synthetic chromogenic substrate (S-2302) for factor XIIa and plasma kallikrein. Bovine histidine-rich glycoprotein inhibits the contact activation induced by both of these activating surfaces.