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Selection of affinity ligands for protein purification from proteolytic digests

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Biotechnology Techniques

Abstract

A simple method for the selection of affinity ligands from proteolytic digests by affinity chromatography is proposed. A small proportion of the peptides in the trypsin digest of bovine serum albumin (BSA) or the pepsin digest of cytochrome are retarded on insulin-immobilised or HSA (human serum albumin)-immobilised affinity columns, respectively. The peptides in these selected fractions can be immobilised onto solid phases and used in affinity chromatography procedures for the purification of insulin or HSA. © Rapid Science Ltd. 1998

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Authors and Affiliations

  1. Institute of Chemistry, Chinese Academy of Sciences, Beijing, China

    Yuhui Yang & Guoquan Liu

  2. Department of Chemical Engineerng, University of Cambridge, Pembroke Street, Cambridge, UK

    Howard A. Chase

Authors
  1. Yuhui Yang
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  2. Howard A. Chase
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  3. Guoquan Liu
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Yang, Y., Chase, H.A. & Liu, G. Selection of affinity ligands for protein purification from proteolytic digests. Biotechnology Techniques 12, 245–251 (1998). https://doi.org/10.1023/A:1008833810721

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  • DOI: https://doi.org/10.1023/A:1008833810721

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