PRIMATE RELAXIN - SYNTHESIS OF GORILLA AND RHESUS-MONKEY RELAXINS

The synthesis of the hormone relaxin from the species Gorilla gorilla (gorilla) and Macaca mulatta (rhesus monkey) has been achieved. Each o f the two chains which constitute the peptide structures was assembled separately, the A-chains (24 amino acids) by the Boc-polystyrene soli d-phase procedure and the B-chains (29 and 28 amino acids) by the Fmoc -polyamide (gorilla) and the Boc-polystyrene (rhesus monkey) solid-pha se methods. After cleavage from the solid supports, the separate chain s were purified to a high degree of homogeneity. Oxidative combination of the respective A- and B-chains in solution at high pH afforded the synthetic relaxins in low overall yield. Chemical and physiochemical characterization of the products confirmed both their purity and their conformational similarity to the human hormone. The synthetic gorilla and rhesus monkey relaxins were both found to possess potent chronotr opic and inotropic activity in the isolated rat cardiac atrium assay.