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Target tissues for relaxin identified in vitro with 125I-labelled porcine relaxin.

Various tissues from the mouse, rat and guinea-pig were used to examine the binding of a biologically active, esterified and 125I-labelled porcine relaxin. Binding to mouse symphysial homogenates was time- and temperature-dependent. Other peptide hormones did not complete with relaxin for binding. Mouse uterine tissue displayed similar binding characteristics. Fractionated mammary tissue from 15- and 20-day-pregnant rats exhibited significant relaxin binding activity, as did homogenates of the guinea-pig public symphysis and cervix. Under the conditions used, no relaxin receptors were noted in the liver, spleen or heart from any of the species investigated.