Primate relaxin: synthesis of gorilla and rhesus monkey relaxins

J Protein Chem. 1994 Apr;13(3):315-21. doi: 10.1007/BF01901564.


The synthesis of the hormone relaxin from the species Gorilla gorilla (gorilla) and Macaca mulatta (rhesus monkey) has been achieved. Each of the two chains which constitute the peptide structures was assembled separately, the A-chains (24 amino acids) by the Boc-polystyrene solid-phase procedure and the B-chains (29 and 28 amino acids) by the Fmoc-polyamide (gorilla) and the Boc-polystyrene (rhesus monkey) solid-phase methods. After cleavage from the solid supports, the separate chains 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 chronotropic and inotropic activity in the isolated rat cardiac atrium assay.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Amino Acids / analysis
  • Animals
  • Cardiotonic Agents / pharmacology
  • Chromatography, High Pressure Liquid / methods
  • Circular Dichroism
  • Gorilla gorilla
  • Heart Atria / drug effects
  • Humans
  • Hydrogen-Ion Concentration
  • In Vitro Techniques
  • Macaca mulatta
  • Male
  • Molecular Sequence Data
  • Myocardial Contraction / drug effects
  • Rats
  • Relaxin / chemical synthesis*
  • Relaxin / genetics
  • Relaxin / isolation & purification
  • Semen / chemistry
  • Sequence Homology, Amino Acid


  • Amino Acids
  • Cardiotonic Agents
  • Relaxin