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We have studied the effect of sulfhydryl agents on the binding of 125I-tyr3-neurotensin to the purified plasma membranes from circular smooth muscle and on the in vitro response of circular muscle strips of canine small intestine to neurotensin. Dithiothreitol (DTT) enhanced the binding by about 80%. Cysteine (a reductant) also enhanced the binding while cystine (an oxidant) reduced the binding to the similar extent. DTT stimulated the tissue in the organ bath and abolished the stimulatory response to low concentrations of neurotensin. The stimulatory response to acetylcholine was not altered by DTT. The implications of the role of disulfide bridges in the neurotensin response is discussed.
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