Histidine-rich glycoprotein inhibits contact activation of blood coagulation.
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.
Vestergaard
A B
AB
Department of Molecular Biology and Plant Physiology, University of Aarhus, Denmark.
Andersen
H F
HF
Magnusson
S
S
Halkier
T
T
D000595:Amino Acid Sequence; D000818:Animals; D001777:Blood Coagulation / Q000187:drug effects*; D002417:Cattle; D006023:Glycoproteins / Q000302:isolation & purification / Q000494:pharmacology*; D006801:Humans; D008969:Molecular Sequence Data; D011506:Proteins / Q000302:isolation & purification / Q000494:pharmacology*; D012689:Sequence Homology, Nucleic Acid; D000099053:Histidine-Rich Glycoprotein
D006023:Glycoproteins; D011506:Proteins; D000099053:Histidine-Rich Glycoprotein