Fusion protein having enhanced in vivo erythropoietin activity

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Glycoprotein – e.g. – mucins – proteoglycans – etc.

Reexamination Certificate

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C530S399000, C435S069100

Reexamination Certificate

active

07091326

ABSTRACT:
Provided is a fusion protein comprising, at its carboxy terminal of human erythropoietin (EPO), a mutant having one to four amino acid substitutions in the carboxy terminal peptide (CTP) fragment of a human chorionic gonadotropin (HCG) β subunit, for increasing an in vivo half-life activity of EPO. The in vivo half-life can be greatly elongated while retaining the intrinsic activity of the EPO, without increasing the sugar chain content.

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Furuhashi et al., “Fusing the Carboxy-Terminal Peptide of the Chorionic Gonadotropin (CG) β-Subunit to the Common α-Subunit: Retention of O-Linked Glycosylation and Enhancedin VivoBioactivity of Chimeric Human CG, Molecular Endocrinology”, 9:1, 54-63 (1995).
Sytkowski et al., “An Erythropoietin Fusion Protein Comprised of Identical Repeating Domains Exhibits Enhanced Biological Properties”, The Journal of Biological Chemistry, 274:35, 24773-24778, 1999.
Communication from Japanese Patent Office.

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