ISSN:
1573-6784
Source:
Springer Online Journal Archives 1860-2000
Topics:
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00159382
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