Isolation and bioactivity of relaxin from the tammar wallaby (Macropus eugenii).

Abstract

Recent cloning of a prepro-relaxin cDNA from the tammar wallaby (Macropus eugenii)[1] indicated that the derived amino acid sequence retains the structural elements common to relaxin peptides from all species, including the three residues that make up the putative receptor binding motif (Fig.1). Although neither marsupial prorelaxin nor relaxin have been extracted and purified from any tissue, early studies demonstrated that crude extracts of corpora lutea (CL) from the pregnant tammar wallaby contain bioactive relaxin [2]. Both the CL and placenta are sites of relaxin mRNA expression during pregnancy in the tammar but transcripts are considerably more abundant in the CL [1]. Within the CL, ..