Baxalta Gmbh

Baxter International Inc.

Baxter Healthcare Sa

Takeda Pharmaceutical Company Limited

Baxter Aktiengesellschaft

Peter Matthiessen

Peter Turecek

Hans-Peter Schwarz

Daniel R Boggs

Thomas R Kreil

Heinz Anderle

Alfred Weber

Kurt Schnecker

Stefan Romeder-Finger

Gerald Brachtl

The present invention relates to formulations of ADAMTS13 with enhanced or desirable properties. As such, the invention provides liquid and lyophilized formulations of ADAMTS13 that are suitable for pharmaceutical administration. Among other aspects, the present invention also provides methods of treating various diseases and conditions related to VWF and/or ADAMTS13 dysfunction in a subject. Also provided herein are kits comprising ADAMTS13 formulations useful for the treatment of various diseases and conditions.

Stabilized liquid and lyophilized ADAMTS13 formulations

The present invention provides long-term stable pharmaceutical formulations of recombinant von-Willebrand Factor (rVWF) and methods for making and administering said formulations.

Recombinant VWF formulations

Methods of preparing alpha-1-antiproteinase inhibitor and controlling the amount of des-lys alpha-1-antiproteinase inhibitor in the preparation, and compositions comprising the same, as well as methods of treatment using the same are provided.

Ethanol dependence of alpha1 antitrypsin C-terminal Lys truncation by basic carboxypeptidases

The present invention relates to a method for determining the highest temperature that is suitable for performing accelerated protein stability studies, as well as to a method for modeling real-time protein stability from accelerated stability data generated at said temperature.

Methods for modeling protein stability

A validatable method for determining a photochemically effective dose for inactivating pathogens in a fluid sample is described herein. In particular, the instant invention covers methods for determining a photochemically effective dose sufficient to inactivate pathogens in a biological sample while leaving biologically active substances of interest unaffected. A batch irradiation reactor effective for inactivating pathogens in biological samples is also described.

Method for the validatable inactivation of pathogens in a biological fluid by irradiation

Ethanol dependence of alpha1 antitrypsin C-terminal lys truncation by basic carboxypeptidases

The present invention relates to a method for determining an effective dose of monochromatic or polychromatic light from one or more light sources to inactivate microorganisms present in a biological fluid, preferably a non-transparent fluid. Moreover, there is provided a method for the inactivation of microorganism in a biological fluid in a flow-through-reactor. Moreover, the invention advantageously provides a flow-through-reactor with one or more thermostated light sources. The invention further provides a method of controlling the light sum dose of monochromatic or polychromatic light emitted from one or more light sources to effectively inactivate microorganisms present in a biological fluid in a batch reactor.

Methods for the inactivation of microorganisms in biological fluids, flow through reactors and methods of controlling the light sum dose to effectively inactivate microorganisms in batch reactors

Recombinant truncated human furin was expressed in CHO cells and concentrated approximately 50-fold by ultrafiltration and diafiltration. The concentrate was purified by column chromatography on CAPTO MMC&#x2122; (mixed cation exchange/hydrophobic interaction gel) resulting in a 30-50 fold purification factor and a yield of at least 60%. The at least 20% pure preparation obtained after CAPTO MMC&#x2122; (mixed cation exchange/hydrophobic interaction gel) chromatography had already a purification degree allowing on-column maturation of pro-VWF. Then an additional Arginine Sepharose chromatography purification was carried out. This two column process for purification of truncated human furin resulted in an almost pure furin preparation with a specific activity of approximately 290,000 U furin/mg protein and a yield of about 50%.

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Vienna, Austria

Peter Matthiessen