Genentech, Inc.

Charles H Schmelzer

Louis E Burton

Joanne T Beck

Shelly Pizarro

Ailen M Sanchez

Jeffrey L Cleland

Anthony J Mason

David W Kahn

Marjorie E Winkler

Michelle D Butler

Processes are provided for recovering and purifying refolded recombinant proteins produced in heterologous host cells, which includes the step of refolding the protein in a high pH buffer.

Refolding of recombinant proteins

A process for recovering and purifying refolded heparin binding proteins produced in heterologous host cells includes the step of incubation of the solubilized protein with a polyanionic species such as dextran sulfate.

Recombinant production of vascular endothelial growth factor

Methods are provided for large scale purification of neurotrophins, including mature NGF, suitable for clinical use. The methods provide means to separate neurotrophins from various less desirable misprocessed, misfolded, size, glycosylated, or charge forms. Compositions of neurotrophins, including mature NGF, substantially free of these variants are also provided.

Isolation of neurotrophins from a mixture containing neurotrophin variants using hydrophobic interaction chromatography

Isolation of neurotrophins from a mixture containing other proteins and neurotrophin variants using hydrophobic interaction chromatography

Purification of NGF

Purification of recombinant human neurotrophins

A pharmaceutical composition and method are provided for erythropoietin therapy, such as treatment of an anemic disease, wherein an effective amount of activin with two beta.sub.B chains formulated in a pharmaceutically acceptable carrier is administered to a patient or animal in need of such therapy. Preferably the activin is human and the composition is administered parenterally.

Purified activin B composition

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Burlingame, CA, United States of America

Charles H Schmelzer