Chiron Corporation

Cephalon, Inc.

Other

Pharmacia & Upjohn Company

Novartis Vaccines & Diagnostics, Gmbh

Patricio T Riquelme

Glenn J Dorin

Cynthia A Cowgill

Russell A Brierley

John M Hanson

Joan N Abrams

Francis C Maslanka

Robert D Kudrna

Christopher M Bussineau

Luis Juarbe-Osorio

Carl Scandella

Mark E Gustafson

Douglas G Bolesch

Asuman G Ozturk

Ausman G Otzurk

Louis Juarbe

David H Reifsnyder

Duane Inlow

Corazon Terciano Victa

Walter Joseph Crosier

John Tharin Wendell

Highly purified preparations of TFPI or TFPI analogs can be prepared using a method that generally involves the following steps: (1) expression of TFPI or TFPI analog in, (2) isolation of refractile bodies, (3) dissolution of the refractile bodies and refolding of the expressed TFPI or TFPI analog, (4) SP-Sepharose fast flow (FF) chromatography, (5) a first concentration and diafiltration step, (6) Q-Sepharose high (HP) performance chromatography, (7) butyl hydrophobic interaction chromatography (HIC), (8) SP-Sepharose HP chromatography, and (9) a second concentration/diafiltration step. Less than about 12% of the TFPI or TFPI analog molecules in such preparations are modified TFPI or TFPI analog species (i.e., oxidized, carbamylated, acetylated, deamidated, aggregated, or misfolded species).

Method of purifying TFPI and TFPI analogs

The present invention is directed to the purification and commercialization of therapeutic polypeptides that have. In one aspect of the invention, a method of purifying Interferon &#x3b2;-1b using size exclusion chromatography is provided. In another aspect of the invention, a method of purifying a polypeptide using size chromatography is provided. A third aspect provides a method of commercializing a polypeptide.

Chromatographic separation of therapeutic polypeptides

Methods for purifying authentic, properly folded IGF polypeptides from yeast transformants are disclosed. The methods include a refolding step and provide for high yields of authentic IGF from a variety of yeast strains.

Methods for purifying authentic IGF from yeast hosts

Methods of purifying authentic IGF from yeast hosts

Disclosed is an improved process for obtaining purified, monomeric, intact, correctly-folded insulin-like growth factor-I (also known as somatomedin-C). The improvements, consisting primarily of the addition of an IGF-I unfolding/refolding step and the substitution of a reverse phase chromatography step for a gel filtration chromatography step result in a three-fold increase in final yield. The process includes the following steps, in order: first cation exchange, unfolding/refolding, hydrophobic interaction chromatography, second cation exchange, and reverse phase chromatography.

IGF-I purification process

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Walnut Creek, CA, United States of America

Patricio T Riquelme