Method for producing mature VWF from VWF pro-peptide

Details Method for producing mature VWF from VWF pro-peptide Method for producing mature VWF from VWF pro-peptide

2008-05-16

2011-11-15

Tsay, Marsha (Department: 1656)

Chemistry: natural resins or derivatives; peptides or proteins;

Proteins, i.e., more than 100 amino acid residues

Separation or purification

C530S350000, C530S380000, C530S417000, C525S054100, C435S069600

Reexamination Certificate

active

08058411

ABSTRACT:
The present invention relates to a method for producing a mature von Willebrand Factor (VWF) from von Willebrand Factor pro-peptide comprising the steps:immobilizing VWF pro-peptide on an ion exchange resin,incubating the immobilized VWF pro-peptide with furin to obtain immobilized mature VWF, andisolating mature VWF from the ion exchange resin by elution.

REFERENCES:
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patent: 2006/0160948 (2006-07-01), Scheiflinger et al.
patent: 0775750 (1997-05-01), None
patent: WO-00/49047 (2000-08-01), None
Cameron et al., Polyarginines are potent furin inhibitors.J. Biol. Chem. 275: 36741-99 (2000).
Leyte et al., The pro-polypeptide of von Willebrand factor is required for the formation of a functional factor VIII-binding site on mature von Willebrand factor.Biochem. J. 274: 257-261 (1991).
Molloy et al., Human furin is a calcium-dependent serine endoprotease that recognizes the sequence Arg-X-X-Arg and efficiently cleaves anthrax toxin protective antigen.J. Biol. Chem. 267: 16396-402 (1992).
Preininger et al., Strategies for recombinant Furin employment in a biotechnological process: complete target protein precursor cleavage.Cytotechnology. 30: 1-15 (1999).
Schlokat et al., Production of highly homogeneous and structurally intact recombinant von Willebrand factor multimers by furin-mediated propeptide removal in vitro.Biotechnol. Appl. Biochem. 24: 257-67 (1996).
Takagi et al., A collagen-binding glycoprotein from bovine platelets is identical to propolypeptide of von Willebrand factor.J. Biol. Chem. 364: 10425-30 (1989).
Than et al., The endoproteinase furin contains two essential Ca2+ions stabilizing its N-terminus and the unique S1 specificity pocket.Acta. Cryst. D61: 505-12 (2005).
International Search Report, International Application No. PCT/US2008/006291, mailed Sep. 1, 2008.
Fischer, “Recombinant von Willebrand factor: Potential therapeutic use,”Journal of Thrombosis and Thrombolysis8: 197-206 (1999).
Fischer et al., “Biochemical and functional characterization of recombinant von Willebrand factor produced on a large scale,”Cell. Mol. Life Sci. 53: 943-950 (1997).

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