Thromb Haemost 1990; 63(03): 517-523
DOI: 10.1055/s-0038-1645076
Original Article
Schattauer GmbH Stuttgart

Proteolytic and Immunologic Comparison of Human and Bovine von Willebrand Factor

Meenakshi R Bakhshi
The Department of Biochemistry and the Thrombosis Research Center, Temple University, Health Sciences Center, Philadelphia, PA, USA
,
Edward P Kirby
The Department of Biochemistry and the Thrombosis Research Center, Temple University, Health Sciences Center, Philadelphia, PA, USA
› Author Affiliations
Further Information

Publication History

Received: 11 April 1989

Accepted after revision 26 January 1990

Publication Date:
30 June 2018 (online)

Summary

The structures of bovine and human vWF were compared by proteolysis with Staphylococcus aureus V8 protease and rattlesnake venom Protease I. Fragments were analyzed for chain composition, heparin binding, collagen binding, platelet agglutinating activity and recognition by a panel of monoclonal antibodies which reacted with both bovine and human vWF. Similar large fragments from the C-terminal domain of vWF were seen in each case. The N-terminal domain resulting from cleavage of bovine vWF was much smaller than that seen upon digestion of human vWF with V8 protease. Protease I destroyed the heparin binding domain in human vWF. Bovine vWF was much less sensitive to proteolysis than was human vWF.