Activation of demineralized bone matrix by genetically engineered human bone morphogenetic protein-2 with a collagen binding domain derived from von Willebrand factor propolypeptide

2006 ◽  
Vol 80A (2) ◽  
pp. 428-434 ◽  
Author(s):  
Bing Chen ◽  
Hang Lin ◽  
Yannan Zhao ◽  
Bin Wang ◽  
Yanhong Zhao ◽  
...  
Keyword(s):  
Von Willebrand Factor ◽  
Demineralized Bone Matrix ◽  
Bone Matrix ◽  
Genetically Engineered ◽  
Bone Morphogenetic Protein 2 ◽  
Collagen Binding ◽  
Morphogenetic Protein ◽  
Human Bone Morphogenetic Protein ◽  
Von Willebrand ◽  
Willebrand Factor

Plasma Derived von Willebrand Factor Preparations: Collagen Binding and Ristocetin Cofactor Activities

1997 ◽  
Vol 78 (02) ◽  
pp. 930-933 ◽  
Author(s):  
Ping Chang ◽  
D L Aronson
Keyword(s):  
Von Willebrand Factor ◽  
Functional Activity ◽  
Binding Activity ◽  
Collagen Binding ◽  
Binding Function ◽  
Cofactor Activity ◽  
Von Willebrand ◽  
Willebrand Factor ◽  
Ristocetin Cofactor ◽  
Ristocetin Cofactor Activity

SummaryFive plasma preparations (11 lots) used in the treatment of von Willebrand’s disease (vWD) were evaluated. The collagen binding function of von Willebrand factor (vWF) containing preparations was compared with the ristocetin cofactor activity and the vWF antigen. Some preparations have higher ratio of functional activity (ristocetin cofactor and collagen binding) relative to the antigen than is found in normal plasma. The ristocetin cofactor activity and the collagen binding activity are tightly correlated (r = .95). Ultracentrifugal (UCF) analysis was used to compare the size distribution of vWf antigen, ristocetin cofactor and collagen binding activity. The sedimentation of all of the vWF parameters in the plasma products was slower than in plasma. In plasma products the ristocetin cofactor activity sediments the most rapidly, the collagen binding activity is slower and the antigen the slowest. The collagen/antigen ratio decreases with decreasing vWF size. Assignment of potency to vWF containing preparations utilizing the collagen binding activity may be more precise and as accurate as with the traditional ristocetin cofactor assay.

Sign in / Sign up

Export Citation Format

Share Document