Medimmune Limited

Medlmmune Limited

Liu Tie

Christopher D Thompson

Alan Hunter

Xiangyang Wang

Timothy Pabst

Mariko Fonseca

Yiming Li

Jared Samuel Bee

Richard Edward Turner

Christopher Douglas Afdahl

David Edwin Gruber

The present invention relates to a method of purifying albumin-fusion proteins to reduce the level of oxidation of susceptible amino acid residues. The method comprises an affinity matrix chromatography step and an anion exchange chromatography step. The purified albumin-fusion proteins have low levels of oxidation and retain their enhanced half-life in vivo and its bioactivity. In some embodiments, the albumin-fusion protein comprises a scaffold, such as human Tenascin C scaffold. Compositions comprising the albumin-fusion protein are further disclosed.

Method of purifying albumin-fusion proteins

Described herein is a method for separating a recombinantly produced polypeptide from host cell protein. The method includes a step of loading a clarified cell culture supernatant that includes the recombinantly produced polypeptide and the HCP onto a Protein A chromatography column and washing the Protein A chromatography column with a wash buffer comprising a fatty acid having a chain length of at least about 6 carbon atoms, or a fatty acid salt thereof to remove HCP and then recovering the recombinantly produced polypeptide.

Purification of recombinantly produced polypeptides

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Gaithersburg, MD, United States of America

Liu Tie