Badgery-Parker T, Lovas S, Conlon J M, Burcher E
School of Physiology and Pharmacology, University of New South Wales, Sydney, Australia.
Peptides. 1993 Jul-Aug;14(4):771-5. doi: 10.1016/0196-9781(93)90112-t.
The tachykinin binding site preferences of neuropeptide gamma (NP gamma), its C-terminal fragments AcNP gamma(3-21), AcNP gamma(5-21), AcNP gamma(7-21), and AcNP gamma(9-21), other mammalian tachykinins, and the nonmammalian tachykinins ranakinin and carassin were examined in membrane binding competition studies. [125I]-Bolton-Hunter [Sar9,Met(O2)11]SP (BHSarSP), [125I]-neurokinin A (INKA) and [125I]-Bolton-Hunter scyliorhinin II (BHScyII) were used to investigate NK-1, NK-2, and NK-3 sites, in rat submandibular gland, gastric fundus, and brain, respectively. Elongation of the neurokinin A molecule does not appear to influence binding to rat tachykinin NK-1 and NK-2 binding sites. Ranakinin has affinity for the NK-1 and NK-2 site similar to that of substance P and neurokinin A, respectively, but has low affinity for the NK-3 site. Despite its structural similarities to neuropeptide gamma, carassin has only moderate affinity for rat tachykinin binding sites. Possession of an acidic residue at position 4 appears critical for binding to rat NK-2 sites.
在膜结合竞争研究中，检测了神经肽γ（NPγ）、其C末端片段AcNPγ(3 - 21)、AcNPγ(5 - 21)、AcNPγ(7 - 21)和AcNPγ(9 - 21)、其他哺乳动物速激肽以及非哺乳动物速激肽蛙皮速激肽和鲤促性腺激素释放激素的速激肽结合位点偏好。分别使用[125I]-博尔顿-亨特[Sar9,Met(O2)11]P物质（BHSarSP）、[125I]-神经激肽A（INKA）和[125I]-博尔顿-亨特猫鲨素II（BHScyII）来研究大鼠颌下腺、胃底和脑中的NK-1、NK-2和NK-3位点。神经激肽A分子的延长似乎不影响其与大鼠速激肽NK-1和NK-2结合位点的结合。蛙皮速激肽对NK-1和NK-2位点的亲和力分别与P物质和神经激肽A相似，但对NK-3位点的亲和力较低。尽管鲤促性腺激素释放激素在结构上与神经肽γ相似，但它对大鼠速激肽结合位点只有中等亲和力。在第4位拥有一个酸性残基似乎对与大鼠NK-2位点的结合至关重要。
