Chang R S, Lotti V J, Chen T B
Merck Sharp & Dohme Research Laboratories, Department of Microbiol Pharmacometrics, West Point, PA 19486.
Biochem Biophys Res Commun. 1988 Mar 30;151(3):1213-9. doi: 10.1016/s0006-291x(88)80495-9.
The binding of biologically active [3H]propionyl-NPY to rabbit aortic membranes was specific and saturable. Scatchard analysis indicated a single class of binding sites with a Kd of 1.1 nM. The rank order of potencies for displacement of [3H]propionyl-NPY binding by NPY analogs in the aorta correlated with their potencies in displacing binding in brain and their activity in inhibiting contractions of the field-stimulated rat vas deferens. However, differences were noted in the absolute or relative potencies of other related polypeptides both in regards to aorta compared to brain NPY binding and NPY binding compared to activity in the vas deferens. Collectively, the results support proposals for heterogeneity of NPY receptors.
具有生物活性的[3H]丙酰基神经肽Y([3H]propionyl-NPY)与兔主动脉膜的结合具有特异性且可饱和。Scatchard分析表明存在一类结合位点,其解离常数(Kd)为1.1 nM。在主动脉中,神经肽Y类似物取代[3H]丙酰基神经肽Y结合的效力排序与其在脑中取代结合的效力以及抑制电场刺激的大鼠输精管收缩的活性相关。然而,在其他相关多肽的绝对或相对效力方面,与脑内神经肽Y结合相比,主动脉存在差异,与输精管活性相比,神经肽Y结合也存在差异。总体而言,这些结果支持了神经肽Y受体存在异质性的观点。