Use of size-exclusion chromatography for refolding recombinant proteins from inclusion bodies

Julian B Chaudhuri, Edward Fahey

Research output: Contribution to journalArticle

Abstract

Refolding recombinant proteins from inclusion bodies is subject to low yields resulting from aggregation of folding intermediates. Redn. in aggregation may be achieved through refolding using a gel filtration matrix. The SEPROS (Size Exclusion Protein Refolding System) technique allows buffer exchange, refolding and aggregate removal in a single operation. Refolding high concns. of model proteins, such as lysozyme and carbonic anhydrase at high concns. (>20 mg/mL) has been successful (Batas and Chaudhuri, Biotech Bioeng 50, 16-23, 1996). The use of this technique to refold urokinase plasminogen activator (uPA) from inclusion bodies will be reported, along with a description of the effect of protein concn., gel filtration matrix type and sample loading on the refolding yield. A quant. mechanism for protein refolding using size exclusion chromatog. will also be presented. [on SciFinder (R)]
Original languageEnglish
Pages (from-to)BIOT-031
JournalAbstracts of Papers, 221st ACS National Meeting, San Diego, CA, United States, April 1-5, 2001
Publication statusPublished - 2001

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