Fusion protein having the enhanced in vivo activity of...

Details Fusion protein having the enhanced in vivo activity of... Fusion protein having the enhanced in vivo activity of...

2011-08-30

2011-08-30

Kim, Alexander (Department: 1656)

Chemistry: natural resins or derivatives; peptides or proteins;

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

Glycoprotein, e.g., mucins, proteoglycans, etc.

C536S023510

Reexamination Certificate

active

08008454

ABSTRACT:
The present invention relates to a fusion protein in which a carboxy terminal of human erythropoietin (EPO) is fused with a carboxy terminal peptide fragment of β subunit of human chorionic gonadotropin (HCG), to DNA encoding the fusion protein, and to a method for preparation of the fusion protein. The fusion protein has the enhanced in vivo activity of erythropoietin.

REFERENCES:
patent: 5585345 (1996-12-01), Boime
patent: 5712122 (1998-01-01), Boime et al.
patent: 5759818 (1998-06-01), Boime
patent: 5792460 (1998-08-01), Boime
patent: 640619 (1995-03-01), None
Matzuk et al., Site specificity of the Chorionic gonadotropin N-Linked oligosaccharides in Signal Transduction., The Journal of Biological Chemistry, 1989, vol. 264, pp. 2409-2414.
PDB 1QFW—B (last viewed on Jul. 23, 2010).
Matzuk et al., The Role of theasparagine-linked Oligosaccharides of the α Subunit in the Secretion and Assembly of Human Chorionic Gonadotropin., The Journal of Cell Biology, 1988, vol. 106, pp. 1049-1059.

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