Synthesis of a pentekontapeptide with high lipolytic activity corresponding to the carboxyl-terminal fifty amino acids of ovine beta-lipotropin.

The synthesis of a peptide, composed of fifty amino-acid residues, corresponding to positions 42-91 in ovine beta-lipotropin has been accomplished by the solidphase method. The preformed symmetrical anhydride and active ester coupling methods were used exclusively. The synthetic product was purified by gel filtration, carboxymethylcellulose chromatography, and partition chromatography on Sephadex G-50. Its lipolytic activity in isolated rabbit fat cells was about six times that of beta-lipotropin on a weight basis.