Summary
Recombinant salmon growth hormone (SGH) expressed inEscherichia coli was refolded and purified. Native form SGH with a purity of 98% was obtained with a recovery of 9%. We found that purified SGH in reduced form under denaturing conditions efficiently formed correct disulfide bonds.
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Sugimoto, S., Yokoo, Y. Purification of recombinant salmon growth hormone expressed inEscherichia coli . Biotechnol Lett 13, 389–394 (1991). https://doi.org/10.1007/BF01030988
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DOI: https://doi.org/10.1007/BF01030988