Tachykinin receptors in chicken intestine were studied using radioligand binding and functional techniques. Mechanisms of tachykinin-induced contraction were also investigated. Binding of [125I]Bolton-Hunter substance P ([125I]BH-SP) to chicken ileal membranes was rapid, saturable, of high affinity and to a single population of binding sites with Kd 0.72 nM and Bmax 0.48 fmol/ wet weight tissue. The rank order of agonists competing for [125I]BH-SP binding sites was [Sar9]SP > [Arg3]SP (natural tachykinin in chickens) > SP > [Pro9]SP > or = NKA > eledoisin > [Sar9,Met(O2)11]SP >> [Lys5,MeLeu9,Nle10]-NKA(4-10) >> senktide, suggesting similarities to the mammalian NK1 receptor. The NK1 receptor antagonist CP 99994, and NK2 receptor antagonist SR 48968 were weak competitors while spantide, RP 67580, GR 82334, GR 94800 and MEN 11420 were ineffective. The radioligand [125I]NKA showed no specific binding to ileal membranes. The potency order of most tachykinins in contacting isolated ileal longitudinal segments was in good agreement with that obtained from competition binding studies. Contractions to [Arg3]SP, NKA and senktide were greatly reduced by tetrodotoxin, suggesting that neurally-mediated responses were primarily involved. [Arg3]SP and NKA acted mainly by increasing release of acetylcholine, prostaglandins and probably tachykinins. Responses to [Arg3]SP were virtually abolished by nifedipine but were unaffected by NK1 receptor antagonists. Senktide-induced contraction was inhibited by the NK3 receptor antagonist, SR 142801, but was unaffected by atropine or L-NAME. The study provides evidence for a tachykinin receptor with similarities to the NK1 receptor in the chicken small intestine. In addition, senktide may act on a receptor similar to the mammalian NK3 receptor.