Abstract: The present invention relates to novel full-length interferon gamma (IFNG) polypeptide variants having interferon gamma activity. The full-length interferon gamma polypeptide variants of the invention are obtained by performing selected modifications in the C-terminal part of the molecule. The full-length interferon gamma polypeptide variants of the invention are useful in therapy, in particular for the treatment of interstitial pulmonary diseases, such as idiopathic pulmonary fibrosis.

Abstract: When interferon gamma (IFNG) is produced in mammalian cell lines a heterogenous population of IFNG polypeptides is obtained due to C-terminal processing of the IFNG polypeptide. Clearly, this constitutes a severe problem in that valuable polypeptide material is lost and, further, it is necessary to carry out time-consuming and cumbersome purification in order to obtain a homogenous population of active IFNG polypeptides having the desired length. It has now been found that an IFNG fragment containing 132 amino acid residues (truncated at the nucleotide level by introducing a stop-codon after the codon encoding amino acid residue no. 132) does not undergo C-terminal truncation or, at least, is not significantly C-terminally truncated. Furthermore, as the IFNG fragment containing 132 amino acid residues is active, this opens up the possibility of producing a homogenous active IFNG polypeptide in eukaryotic host cells, such as CHO cells.

Abstract: Glycosylated polypeptides comprising the primary structure NH2-X-Pp-COOH, wherein X is a peptide addition comprising or contributing to a glycosylation site, and Pp is a polypeptide of interest or comprising the primary structure NH2-Px-X-Py-COOH, wherein Px is an N-terminal part of a polypeptide Pp of interest, Py is a C-terminal part of said polypeptide Pp, and X is a peptide addition comprising or contributing to a glycosylation site are provided. The glycosylated polypeptides possess improved properties as compared to the polypeptide of interest.

Abstract: The present invention relates to novel full-length interferon gamma (IFNG) polypeptide variants having interferon gamma activity. The full-length interferon gamma polypeptide variants of the invention are obtained by performing selected modifications in the C-terminal part of the molecule. The full-length interferon gamma polypeptide variants of the invention are useful in therapy, in particular for the treatment of interstitial pulmonary diseases, such as idiopathic pulmonary fibrosis.

Abstract: When interferon gamma (IFNG) is produced in mammalian cell lines a heterogenous population of IFNG polypeptides is obtained due to C-terminal processing of the IFNG polypeptide. Clearly, this constitutes a severe problem in that valuable polypeptide material is lost and, further, it is necessary to carry out time-consuming and cumbersome purification in order to obtain a homogenous population of active IFNG polypeptides having the desired length. It has now been found that an IFNG fragment containing 132 amino acid residues (truncated at the nucleotide level by introducing a stop-codon after the codon encoding amino acid residue no. 132) does not undergo C-terminal truncation or, at least, is not significantly C-terminally truncated. Furthermore, as the IFNG fragment containing 132 amino acid residues is active, this opens up the possibility of producing a homogenous active IFNG polypeptide in eukaryotic host cells, such as CHO cells.

Abstract: The invention relates to a single-chain oilgomeric polypeptide antagonist which binds to an extracellular ligand-binding domain of a cellular receptor of a type requiring binding of an oligomeric ligand to two or more receptor subunits to be activated, the polypeptide comprising at least two, typically structurally homologous, receptor-binding sites of which at least one is capable of binding to a ligand-binding domain of the cellular receptor and at least one is incapable of effectively binding to a ligand-binding domain of the cellular receptor, whereby the single-chain oligomeric polypeptide is capable of binding to the receptor, but incapable of activating the receptor; as well as to nucleotide sequences encoding such single-chain oligomeric polypeptides, expression vectors comprising such a nucleotide sequence, recombinant host cells comprising such a nucleotide sequence or expression vector, methods for producing the nucleotide sequences and polypeptides, pharmaceutical compositions comprising the singl

Abstract: When interferon gamma (IFNG) is produced in mammalian cell lines a heterogenous population of IFNG polypeptides is obtained due to C-terminal processing of the IFNG polypeptide. Clearly, this constitutes a severe problem in that valuable polypeptide material is lost and, further, it is necessary to carry out time-consuming and cumbersome purification in order to obtain a homogenous population of active IFNG polypeptides having the desired length. It has now been found that an IFNG fragment containing 132 amino acid residues (truncated at the nucleotide level by introducing a stop-codon after the codon encoding amino acid residue no. 132) does not undergo C-terminal truncation or, at least, is not significantly C-terminally truncated. Furthermore, as the IFNG fragment containing 132 amino acid residues is active, this opens up the possibility of producing a homogenous active IFNG polypeptide in eukaryotic host cells, such as CHO cells.

Abstract: Glycosylated polypeptides comprising the primary structure NH2—X—Pp—COOH, wherein X is a peptide addition comprising or contributing to a glycosylation site, and Pp is a polypeptide of interest or comprising the primary structure NH2-Px—X—Py-COOH, wherein Px is an N-terminal part of a polypeptide Pp of interest, Py is a C-terminal part of said polypeptide Pp, and X is a peptide addition comprising or contributing to a glycosylation site are provided. The glycosylated polypeptides possess improved properties as compared to the polypeptide of interest.

Abstract: Heterodimeric polypeptide conjugates exhibiting FSH activity, comprising a dimeric polypeptide comprising an FSH-&agr; subunit and an FSH-&bgr; subunit, wherein at least one of the FSH-&agr; and FSH-&bgr; subunits differs from the corresponding wildtype subunit in that at least one amino acid residue acid residue comprising an attachment group for a non-polypeptide moiety has been introduced or removed, and having at least one non-polypeptide moiety bound to an attachment group of at least one of said subunits are provided. Preferably, at least one attachment group, e.g., an N- or O-glycosylation site or an attachment site for a polymer molecule such as polyethylene glycol, has been introduced, e.g., at an N-terminal. The polypeptide conjugates exhibit improved properties, in particular an increased half-life, compared to human FSH.