Synthesis of the C-terminal decapeptide of bovine insulin B-chain.
The liquid-phase synthesis of a decapeptide corresponding to the last 10 amino acid residues of bovine insulin B-chain is described. Modified monofunctional polyethylene glycol containing benzyl bromide functional group was used as the soluble polymeric support. Cleavage of the fully-protected peptide from the polymer was achieved with 1N NaOH in dioxane. The protected peptide was purified by chromatography on Sephadex LH-20. The protecting groups of a sample were removed with anhydrous HF, and the unprotected crude decapeptide was purified by ion-exchange chromatography on carboxymethyl-cellulose. Both peptides were tested for the racemization of individual amino acids by the gas chromatographic method. The results showed that no residue had been significantly racemized.
D000818:Animals; D002417:Cattle; D002849:Chromatography, Gas; D002855:Chromatography, Thin Layer; D007328:Insulin / Q000138:chemical synthesis*; D008722:Methods; D009842:Oligopeptides / Q000138:chemical synthesis*
D007328:Insulin; D009842:Oligopeptides