Journal article

Solid-phase synthesis of ovine Leydig cell insulin-like peptide - a putative ovine relaxin?

NF Dawson, YY Tan, M Macris, L Otvos, RJ Summers, GW Tregear, JD Wade

JOURNAL OF PEPTIDE RESEARCH | MUNKSGAARD INT PUBL LTD | Published : 1999

Abstract

The primary structure of ovine Leydig cell insulin-like peptide (Ley I-L) was recently deduced from the corresponding cDNA sequence. It consists of two peptide chains and three disulphide bonds in an arrangement similar to both relaxin and insulin. As in relaxin B-chain, an Arg-X-X-X-Arg sequence exists within the Ley I-L B-chain although it is located four residues towards the C-terminus from the corresponding position within relaxin. This sequence of amino acids is known to be essential for relaxin biological activity and its presence in Ley I-L suggested that the peptide might possess a relaxin-like function. Ovine Ley I-L was assembled by Fmoc-solid-phase synthesis of the separate chains..

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