Abstract
First total synthesis of a nonatetracontapeptide corresponding to the entire amino acid sequence of thymopoietin II, a T cell differentiating hormone isolated from bovine thymus, was described. Toward the synthesis of this hormone, two relatively large fragments corresponding to the sequence 1-27 and 28-49 were prepared and the fragments were served as the building blocks for the final construction of the entire amino acid sequence of the hormone. The final deprotection of the fully protected nonatetracon-tapeptide was achieved by the treatment with methanesulfonic acid or hydrogen fluoride, and the purification of the synthetic peptide was effected by a column chromatography on Sephadex G-50, Biogel P-2 and CM-cellulose. The physicochemical and biological properties of the synthetic peptide were also described.
