Chiron Corporation

Cephalon, Inc.

Other

Carl Scandella

Nancy L Haigwood

Glenn J Dorin

Cynthia A Cowgill

Russell A Brierley

Patricio T Riquelme

John M Hanson

Francis C Maslanka

Joan N Abrams

Christopher M Bussineau

Robert D Kudrna

Luis Juarbe-Osorio

Asuman G Ozturk

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

A method for purifying recombinant HIV gp120 so as to provide a glycopeptide having protein/protein binding properties substantially identical to natural viral HIV gp120, which comprises fractionating a composition containing crude gp120 sequentially using (1) ion exchange chromatography, (2) hydrophobic-interaction chromatography, and (3) size exclusion filtration, collecting at each step a fraction that exhibits specific binding affinity for CD4 peptide. The process is carried out in the absence of any affinity purification steps or any steps (such as reverse-phase HPLC) that use contact protein with organic solvents. The product obtained by this method is a purified, full-length, non-fusion recombinant HIV gp120 glycoprotein having protein/protein interaction properties substantially identical to gp120 as presented on an HIV virus, including binding affinity for CD4 and binding affinity for at least one antibody capable of neutralizing HIV infectivity.

Purified GP120 composition retaining natural conformation

A method for purifying recombinant HIV gp120 so as to provide a glycopeptide having protein/protein binding properties substantially identical to natural viral HIV gp120, which comprises fractionating a composition containing crude gp120 sequentially using (1) ion exchange chromatography, (2) hydrophobic-interaction chromatography, and (3) size exclusion filtration, collecting at each step a fraction that exhibits specific binding affinity for CD4 peptide. The process is carried out in the absence of any affinity purification steps or any steps (such as reverse-phase HPLC) that use contact protein with organic solvents. The product obtained by this method is a purified, full-length, non-fusion recombinant HIV gp120 glycoprotein having protein/protein-interaction properties substantially identical to gp120 as presented on an HIV virus, including binding affinity for CD4 and binding affinity for at least one antibody capable of neutralizing HIV infectivity.

Purified gp120 composition retaining natural conformation

Purified gp120 compositions retaining natural conformation

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Oakland, CA, United States of America

Carl Scandella