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- W2046417618 abstract "To determine whether neutral endopeptidase regulates the binding of substance P to the receptors, and if so, what the mechanism is, we determined the effect of neutral endopeptidase inhibitors, thiorphan and phosphoramidon, on specific binding of 3H-substance P to homogenates of rat ileum. Specific binding was of high affinity and was saturable (dissociation constant, KD = 2.4 +/- 0.17 nM and number of maximal binding sites, Bmax = 101.1 +/- 5.5 fmol/mg protein), and the receptor subtype was substance P-P type. Neutral endopeptidase inhibitors increased the specific binding to up to 160% of control (P less than 0.005). Neutral endopeptidase inhibitors prevented the degradation of 3H-substance P during the binding assay and increased the amount of 3H-substance P remaining in the assay system to up to 4.5-fold of control (P less than 0.005), but did not significantly change the KD or Bmax values of specific binding. Protease inhibitors of kininase II, serine proteinases, or thiol proteinases did not significantly change either specific binding or the amount of 3H-substance P remaining in the assay system. We conclude that neutral endopeptidase regulates the binding of substance P to the receptors and that it does so by decreasing the amount of substance P available to the receptors, without significantly changing the affinity or the number of receptors." @default.
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- W2046417618 date "1988-05-01" @default.
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- W2046417618 title "Effect of neutral endopeptidase inhibitors on 3H-substance P binding in rat lleum" @default.
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- W2046417618 doi "https://doi.org/10.1016/0143-4179(88)90074-1" @default.
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