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Biochemistry. 2002 Jan 8;41(1):274-81.

The primary structure and the disulfide links of the bovine relaxin-like factor (RLF).

Author information

1
Department of Biochemistry and Molecular Biology, Medical University of South Carolina, 173 Ashley Avenue, PO Box 250509, Charleston, South Carolina 29425, USA. bullesee@musc.edu

Abstract

The relaxin-like factor (RLF), produced by the Leydig cells, is an essential link in the chain of events leading to the proper positioning of the testes during fetal development. The primary structure of RLF, as reported in the literature, is based solely upon cDNA sequences with chain lengths determined according to deduced processing sites and with relaxin-like cross-links. Biochemical characterization of bovine testicular RLF shows clearly that the endogenous hormone does consist of a 26 residue A chain and two forms of B chain, one containing 40 residues, the other 45. In addition, both B chains are 9 residues longer at the C terminus than the cDNA-deduced chain, and about 20% of the B chains have an additional 5 residue extension at the N terminus. Sequence analysis in combination with mass spectrometry and tryptic peptide mapping showed unambiguously that RLF is larger than previously assumed and that it has the relaxin-type disulfide bond distribution that makes it a bona fide member of the relaxin family of hormones.

PMID:
11772026
DOI:
10.1021/bi0117302
[Indexed for MEDLINE]

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