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Comparision of the methods available for the purification of hybrid β-galactosidase proteins produced under the control of an anaerobically-induced promoter

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Biotechnology Techniques

Summary

Various methods available for purifying β-galactosidase fusion proteins were compared in an attempt to purify a hydrophobic hybrid protein, NirC' 'LacZ, produced under the control of an anaerobically-induced promoter. Conventional ion-exchange techniques and affinity chromatography on p-aminobenzyl-thiogalactoside Sepharose CL-4B, supplied by Sigma Chemical Co., were unsatisfactory. In contrast, immunoaffinity chromatography on anti-β-galactosidase ProtosorbTM, obtained from Promega Biotech, or with immnunoadsorbents prepared in our laboratory, produced a purified hybrid protein which was suitable for N-terminal amino acid analysis.

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Mohan, S.B., Woods, N., Lyddiatt, A. et al. Comparision of the methods available for the purification of hybrid β-galactosidase proteins produced under the control of an anaerobically-induced promoter. Biotechnol Tech 4, 379–384 (1990). https://doi.org/10.1007/BF00159382

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  • DOI: https://doi.org/10.1007/BF00159382

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