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Efficient purification and analysis for stability of human secretin precursor-like peptide produced inEscherichia coli

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Summary

A gene coding for human secretin elongated at the C-terminus by Gly-Lys-Arg, designated as SeeGKR gene, was fused to downstream of an artificial human growth hormone gene and expressed inEscherichia coli. After cleavage of the fusion product with cyanogen bromide (CNBr), the desired SecGKR was purified to homogeneity at a high recovery using a convenient method established in the present study. The SecGKR was hard broken down in aqueous solution, comparing with the mature secretin.

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Author notes

  1. Fusakazu Misoka

    Present address: Technology Center of Nagasaki, 2-1303-8, Ikeda-cho, Omura, Nagasaki 856, Japan

Authors and Affiliations

  1. Institute for Biotechnology Research, Wakunaga Pharmaceutical Co., Ltd., 1624, Shimokodachi, Koda-cho, Takata-gun, 729-64, Hiroshima, Japan

    Fusakazu Misoka & Toru Fuwa

  2. Institute of Pharmaceutical Sciences, Hiroshima University School of Medicine, Kasumi 1-2-3, Minami-ku, Hiroshima 734, Japan

    Masanori Sugiyama

Authors
  1. Fusakazu Misoka
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  2. Masanori Sugiyama
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  3. Toru Fuwa
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Misoka, F., Sugiyama, M. & Fuwa, T. Efficient purification and analysis for stability of human secretin precursor-like peptide produced inEscherichia coli . Biotechnol Lett 13, 603–608 (1991). https://doi.org/10.1007/BF01033418

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