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Title: Synthesis of the C-terminal decapeptide of bovine insulin B-chain. Author: Hemmasi B, Woiwode W, Bayer E. Journal: Hoppe Seylers Z Physiol Chem; 1979 Dec; 360(12):1775-81. PubMed ID: 393606. Abstract: 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.[Abstract] [Full Text] [Related] [New Search]