Protein complexes having factor VIII:C activity and production t

Chemistry: molecular biology and microbiology – Micro-organism – tissue cell culture or enzyme using process... – Recombinant dna technique included in method of making a...

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4351723, 4352402, 4353201, 530383, 536 235, 930100, C07K 14755, C12N 510, C12N 1512, C12N 1563

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057892032

ABSTRACT:
Recombinant protein complexes having human Factor VIII:C activity are expressed in a eukaryotic host cell by transforming the host cell with first and second expression cassettes encoding a first polypeptide substantially homologous to human Factor VIII:C A domain and a second polypeptide substantially homologous to human Factor VIII:C C domain, respectively. In the present invention, the first polypeptide may be extended having at its C-terminal a human Factor VIII:C B domain N-terminal peptide, a polypeptide spacer of 3-40 amino acids, and a human Factor VIII:C B domain C-terminal peptide. Expression of the second polypeptide is improved by employing an .alpha..sub.1 -antitrypsin signal sequence.

REFERENCES:
patent: 4657894 (1987-04-01), Zimmerman
patent: 4757006 (1988-07-01), Toole et al.
patent: 4868112 (1989-09-01), Toole
patent: 4965199 (1990-10-01), Capon et al.
patent: 5004804 (1991-04-01), Kuo et al.
patent: 5045455 (1991-09-01), Kuo et al.
patent: 5084390 (1992-01-01), Hallewell
patent: 5149637 (1992-09-01), Scandell et al.
patent: 5171844 (1992-12-01), van Ooyen et al.
patent: 5198349 (1993-03-01), Kaufman
Burke et al. "The functional domains of coagulation factor VIII:C" (1986) J. Biol. Chem. 261:12574-12578.
Eaton et al. "Construction and characterization of an active factor VIII variant lacking the central one-third of the molecule" (1986) Biochemistry 25:8343-8347.
Fulcher et al. "Human factor VIII procoagulant protein: Monoclonal antibodies define precursor-product relationships and functional epitopes" (1985) J. Clin. Invest. 76:117-124.
Gitschier et al. "Characterization of the human factor VIII gene" (1984) Nature 312:326-330.
Nordfang et al. "Generation of active coagulation factor VIII from isolated subunits" (1988) J. Biol. Chem. 263:1115-1118.
Orr et al. "`Spacer` function implied for the heavily glycosylated region of factor VIII" (1985) J. Inter. Soc. Throm. Hemo. 54:S321 (abstract).
Rotblat et al. "Purification of human factor VIII:C and its characterization by western blotting using monoclonal antibodies" (1985) Biochemistry 24:4294-4300.
Toole et al. "Molecular cloning of a cDNA encoding human antihaemophilic factor" (1984) Nature 312:342-347.
Truett et al. "Characterization of the polypeptide composition of human factor VIII:C and the nucleotide sequence and expression of the human kidney cDNA" (1985) DNA 4:333-349.
Vehar et al. "Structure of human factor VIII" (1984) Nature 312:337-342.
Wood et al. "Expression of active human factor VIII from recombinant DNA clones" (1984) Nature 312:330-337.
Yonemura et al. (1993) "Efficient production of recombinant human factor VIII by co-expression of the heavy and light chains" Protein Engineering vol. 6, No. 6, pp. 669-674.
Burke, R.L. et al. J. Biol. Chem. 261(27):12574-12578 (1986).
Pavirani, A. et al. Biochem. Biophys. Res. Comm. 145(1): 234-240 (1987).
Toole, J.J. et al. PNAS 83:5939-5942 (1986).

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