Synthesis of a biologically active truncated insulin. Des(pentapeptide B26–30) human (porcine) insulin
- 1 January 1974
- journal article
- Published by Royal Society of Chemistry (RSC) in Journal of the Chemical Society, Perkin Transactions 1
- Vol. 11, 1311-1317
- https://doi.org/10.1039/p19740001311
Abstract
An analogue of human (porcine) insulin which differs from the parent molecule in that the C-terminal pentapeptide sequence of the B chain has been eliminated has been synthesized. For this purpose, des(pentapeptide B26–30) B chain S-sulphonate was synthesized by the fragment condensation approach and isolated in highly purified form. Interaction of this compound with the thiol form of the A chain of human (porcine) insulin yielded des(p entapeptide B26–30) human (porcine) insulin, which was purified by chromatography on a carboxymethylcellulose column with an exponential sodium chloride gradient. The des(pentapeptide B26–30) insulin shows potencies of 8·5–9 I.U. mg–1 when assayed by the mouse convulsion method and of 11 I.U. mg–1 by the radioimmunoassy method (cf. 23–25 I.U. mg–1 for the natural hormone). This indicates that the C-terminal pentapetide sequence of the B chain does not participate functionally in the mechanism of the action of insulin.Keywords
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