Abstract
The semisynthesis of deshexapeptide insulin (DHI) from desoctapeptide insulin (DOI) reported earlier1 showed that DHI was biologically active. However, the product was not quite homogeneous, mainly due to the esterification side reaction and the following saponification2. Recently, the catalytic action of trypsin was successfully used in the preparation of human insulin from porcine insulin3. It was also used in the preparation of insulin analogues with substitutions of B24 or B25 phenylalanine by leucine4,5. Here, we report the synthesis of DHI from DOI and glycylphenylalanine through the catalytic action of trypsin. The product, purified by gel filtration and DEAE-Sephadex ion-exchange chromatography, showed insulin activity of 7.5 IU mg−1 in vivo and could be obtained in crystalline form.
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References
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Cao, Q., Cui, D. & Zhang, Y. Enzymatic synthesis of deshexapeptide insulin. Nature 292, 774–775 (1981). https://doi.org/10.1038/292774a0
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DOI: https://doi.org/10.1038/292774a0
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