Abstract: Aspects of the present invention relate to the recombinant production of a mature complement system protein. Certain embodiments of the present invention relate to recombinant production of fully mature human complement Factor I protein (CFI). Included herein are details of an expression vector with which to recombinantly express fully mature human CFI from mammalian cells. Further disclosed are chromatography steps with which to purify recombinantly expressed CFI. Certain aspects of the present invention relate to the use of an expression system in gene therapy and the like. Certain embodiments of the present invention relate to use of said vector as a medicament, for example for use in the treatment of complement-mediated disorders.

Abstract: A therapeutic reagent to control one or more reactions of the immune system in a host, or to deliver anti-tumour agents, or disease treatment agents to the host. The therapeutic reagent comprises a regulatory moiety and a carrier protein that inactivates or substantially reduces the activity of the regulatory moiety. Also, the therapeutic reagent includes a cleavage site at which cleavage of the therapeutic reagent can occur to free the regulatory moiety from the carrier protein so that the therapeutic reagent can act at a diseased site in the host.

Abstract: The three-dimensional structure of human chorionic gonadotrophin (hCG) has been determined by X-ray crystallography and the coordinates of the individual atoms are presented. Analogues of hCG and other glycoprotein hormones sharing a similar .alpha.-subunit structure are produced by inputting chemical changes to the structure into a computer loaded with three-dimensional molecular simulation software and representing visually on a computer display. The three-dimensional structures of the original glycoprotein and the chemically modified analogues are compared, and those analogues wherein the three-dimensional configuration and spatial arrangement of regions involved in receptor binding and signal transduction remain substantially preserved are selected for synthesis by molecular biology techniques and screening for biological activity. Glycoprotein analogues with additional glycosylation sites, and deletion of non-essential hairpins are disclosed.