Abstract: Conjugates exhibiting growth hormone (GH) activity and comprising at least one non-polypeptide moiety covalently attached to a GH polypeptide, the amino acid sequence of which differs from that of wildtype human GH in at least one introduced and at least one removed amino acid residue comprising an attachment group for said first non-polypeptide moiety. The first non-polypeptide moiety is e.g. a polymer molecule such as PEG or a sugar moiety. The conjugate finds particular use in therapy.

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.