作者: Dipankar Das , Theresa M. Allen , Mavanur R. Suresh
DOI: 10.1016/J.PEP.2004.10.007
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摘要: Abstract Different chromatographic methods have been used to purify bacterially expressed single chain antibodies in soluble or insoluble form. Here, we compared two for purification of anti-CD19-c-myc-His6-Cys scFv Escherichia coli as protein. The protein-L–agarose method is a one step that yielded significant amounts pure protein the two-step Ni–NTA–agarose plus Resource 15S method. However, protein-L exhibited an additional lower molecular weight contaminant. Based on results from vitro gel digestion, mass spectrometry and database search results, confirmed contaminant, which could not be purified by column method, degraded product full length construct.