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. 2018 Nov 4;35(1):e2732. doi: 10.1002/btpr.2732

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© 2018 The Authors. Biotechnology Progress published by Wiley Periodicals, Inc. on behalf of American Institute of Chemical Engineers.

This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited and is not used for commercial purposes.

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Cathepsin L exists in different CHO cell culture fluids (CCFs) and cleaves variety of recombinant proteins. (A) Fragmentation of Fab A by Cathepsin L isolated from different CHO CCFs as visualized by HP‐SEC profiles. CCFs were obtained from bioreactors operated with CHO cells expressing therapeutic proteins (Fab B, IgG1, and Bis A), purified with affinity chromatography to deplete the therapeutic protein, and then Cathepsin L was captured from the affinity unbound fraction with CEX. (B) Fragmentation (during pH 3.4 incubation) visualized by HP‐SEC profiles for Fabs (B and C), mAbs (IgG1, 2 and 4), Bi‐specific (BIS A and B), a mAb‐fusion protein (mAb FP) and an albumin‐fusion protein (albumin FP). (C) Fragmentation (during pH 3.4 incubation) visualized by HP‐SEC profiles for IgG1 captured from CCF by Fractogel® EMD SO₃(M) and MabSelect™ SuRe.