Novo Nordisk A/s

Novo Industri A/s

Novo Nordiskals

Noyo Nordisk A/s

Lars Thim

Ole Hvilsted Olsen

Per Balschmidt

Kjeld Norris

Hans Holmegaard So Slashedrensen

Gert Bolt

Jesper Zeuthen

Mogens Christensen

Shawn DeFrees

Fanny Norris

Thorkild Christensen

Henning Ralf Stennicke

Susanne Bang

Thomas Dock Steenstrup

Karin D Jorgensen

Alister J Moody

Brian Berg Stidsen Vandahl

Martin Edward Judge

Mogens H Nissen

Mogens T Hansen

Flemming S Larsen

Sven Hastrup

Jan Markussen

Kjeld Madsen

Nils Langeland Johansen

Niels Christian Kaarsholm

Jens Juul Holst

So Slashedren Bjo Slashedrn

Birgitte Schjellerup Wulff

Per Franklin Nielsen

Jesper Haaning

Marianne Hjortnes Kjalke

Peter Thygesen

Birgitte Koch Michelsen

Christian Rischel

Klavs H Jorgensen

Anette Sams Nielsen

Ole Dragsbaek Madsen

Jens Jacob Hansen

Niels P Moller

Niels Fiil

Hans O Voigt

Gustav Ammerer

Christensen Thorkild

Peter Kristensen

Kennet Christiansen

Ditte Maria Karpf

Johan Karlsson

Frederik Rode

Kirstine Roepstorff

Maj Petersen

Ole Madsen

Martin Judge

Jens Holst

The present invention relates to B-domain truncated Factor VIII molecules with a modified circulatory half life, said molecule being covalently conjugated with a hydrophilic polymer. The invention furthermore relates to methods for obtaining such molecules as well as use of such molecules.

Conjugated factor VIII molecules

The present invention relates to Von Willebrand (VWF) compounds as well as compositions suitable for treatment of blood clotting diseases. The present invention also relates to pharmaceutical compositions, freeze-dried or liquid, comprising (i) a Factor VIII molecule and (ii) a VWF compound.

Compounds suitable for treatment of haemophilia

A method for purifying a recombinant protein using a multimodal or mixed mode resin containing ligands which comprise a hydrophobic part and a negatively charged part is described. The invention is advantageous in that it is a single step chromatographic process which does not require adjustment of pH or conductivity during loading step and results in high yield and potency. The process is used for the purification of recombinant compositions of coagulation factor, particularly recombinant Factor VIII.

Purification of factor VIII using a mixed-mode or multimodal resin

The present invention relates to novel human glucagon-like peptide-2 (GLP-2) peptides and human glucagon-like peptide-2 derivatives which have a protracted profile of action as well as polynucleotide constructs encoding such peptides, vectors and host cells comprising and expressing the polynucleotide, pharmaceutical compositions, uses and methods of treatment.

GLP-2 compounds, formulations, and uses thereof

The present invention relates to a polypeptide with appetite regulating function/activity, a nucleic acid construct encoding the polypeptide and a method of producing the polypeptide. The invention further relates to recombinant vectors comprising the nucleic acid construct encoding the polypeptide, recombinant host cells comprising the nucleic acid construct or the recombinant vector.

Polypeptide with appetite regulating activity

A pharmaceutical formulation comprising a growth hormone pretreated with zinc and optionally lysine or calcium ions shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Pharmaceutical formulation of human-growth hormone pretreated with zinc

The present invention relates to appetite-suppressing peptides or an appetite-suppressing peptide-containing fraction for the treatment of obesity or type II diabetes.

Use of a pharmaceutical composition comprising an appetite-suppressing

Human spasmolytic polypeptide in glycosylated form

A pharmaceutical formulation comprising a growth hormone and Leu-His-Leu as additive or buffering substance shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Pharmaceutical formulation

A pharmaceutical formulation comprising a growth hormone and Lys-Gly-Asp-Ser (SEQ ID No: 1) as additive or buffering substance shows a very high stability against deamidation, oxidation and cleavage of peptide bonds. The stability of the product allows for the storing and shipment thereof in a lyophilized state or in the form of a dissolved or re-dissolved formulation at ambient temperature.

Substantially pure modified .beta..sub.2 -microglobulin (m.beta..sub.2 m) of the formula I ##STR1## wherein R.sub.1 is 24-amino acid residue, with the sequence Ile-Gln-Arg-Thr-Pro-Lys-Ile-Gln-Val-Tyr-Ser-Arg-His-Pro-Ala-Glu-Asn-Gly-Ly s-Ser-Asn-Phe-Leu-Asn, R.sub.2 is a 30-amino acid residue with the sequence Tyr-Val-Ser-Gly-Phe-His-Pro-Ser-Asp-Ile-Glu-Val-Asp-Leu-Leu-Lys-Asn-Gly-Gl u-Arg-Ile-Gly-Lys-Val-Glu-His-Ser-Asp-Leu-Ser, R.sub.3 is a 20-amino acid residue with the sequence Trp-Ser-Phe-Tyr-Leu-Leu-Tyr-Tyr-Glu-Phe-Thr-Pro-Thr-Glu-Lys-Asp-Glu-Tyr-Al a, R.sub.4 is a 19-amino acid residue with the sequence Arg-Val-Asn-His-Val-Thr-Leu-Ser-Gln-Pro-Lys-Ile-Val-Lys-Trp-Asp-Arg-Asp-Me t, X is Phe, Phe-Ser, or Phe-Ser-Lys, and Y is Asp, Lys-Asp, or Ser-Lys-Asp is disclosed. The presence of the protein in body fluids is a diagnostic and/or prognostic marker for the development of a variety of disorders such as different types of cancer and diseases involving the immune system. Also disclosed are specific anti-m.beta..sub.2 m antibodies used for the detection and quantification of m.beta..sub.2 m.

Modified .beta..sub.2 -microglobulin

Human insulin precursors containing the peptide chain B(1-29)-A(1-21) of human insulin and derivatives thereof with a bridging chain connecting the carboxyl terminus of the B(1-29)-chain with the amino terminus of the A(1-21)-chain are prepared by culturing a yeast host transformed with a replicable expression vehicle capable of expressing a DNA-sequence encoding the insulin precursor. The bridging chain is preferably relatively short and contains preferably from 2 to 8 amino acid residues. The bridging chain must not contain two adjacent basic amino acid residues (Lys or Arg) and has one Lys or Arg connected to the amino terminus of the A(1-21)-chain. Human insulin is prepared from the insulin precursors by in vitro conversion.

DNA-sequence encoding biosynthetic insulin precursors and process for

Glucagon or fragments or derivatives thereof are prepared by cultivation of a yeat strain transformed with a replicable expression vehicle comprising a gene encoding the expression of such products. Synthetic genes encoding glucagon or derivatives thereof have been constructed. Also provided are replicable expression vehicles comprising a replication system for providing stable maintenance in yeast and a DNA-sequence encoding glucagon or fragments or derivatives thereof and transformant yeast strains containing such expression vehicles.

Process for preparing glucagon or fragments or derivatives thereof in

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Gentofte, Denmark

Lars Thim