These tactics depend primarily on coupling of a highly polar compound, as a highly polar handle in the purification process, with the terminal amino group of the desired sequence assembled on a solid support. Lysine was used as the highly polar compound in this study. All protecting groups labile towards hydrogen fluoride were removed as usual and the resulting crude peptide was purified through a carboxymethyl cellulose column. The amino terminal lysine residue was removed by Edman degradation to obtain the desired peptide. The technique thus developed has permitted the syntheses of peptide fragments of the B chain of human insulin, H-Gly-Phe-Phe-Tyr-Thr-Pro-Lys (Tfa)-Thr-OH and H-Gly-Ser-His-Leu-Val-OH, with a simple purification process in good yield and in high purity.