Schalling M, Neil A, Terenius L, Lindgren J A, Miamoto T, Hökfelt T, Samuelsson B
Eur J Pharmacol. 1986 Mar 18;122(2):251-7. doi: 10.1016/0014-2999(86)90110-x.
Binding sites for [3H]LTC4 were observed in crude membrane preparations of rat central nervous system tissue. Equilibrium binding studies indicated one high affinity [3H]LTC4 binding site with a KD of 31.4 +/- 3.4 nM for whole brain preparations. The binding was highly specific for [3H]LTC4 and could be inhibited by the SRS-A antagonist FPL 55172. Specific binding was increased with both mono- and di-valent ions. Regional distribution studies revealed a three-fold difference in binding capacity within different regions of the brain with the highest binding capacity in the brainstem (94.1 +/- 6.9 fmol/mg of protein) and the lowest in the hypothalamus (29.6 +/- 12.8 fmol/mg of protein). In addition, weak low capacity binding was observed for [3H]LTB4 and [3H]LTE4, while no saturable binding was observed for [3H]LTD4. The order of selectivity in inhibiting [3H]LTC4 binding was LTC4 much greater than LTD4 = LTE4 greater than LTB4.
在大鼠中枢神经系统组织的粗制膜制剂中观察到了[3H]LTC4的结合位点。平衡结合研究表明，全脑制剂存在一个高亲和力的[3H]LTC4结合位点，解离常数（KD）为31.4±3.4 nM。该结合对[3H]LTC4具有高度特异性，且可被慢反应物质A（SRS-A）拮抗剂FPL 55172抑制。单价和二价离子均可增加特异性结合。区域分布研究显示，脑内不同区域的结合能力存在三倍差异，其中脑干的结合能力最高（94.1±6.9 fmol/mg蛋白质），下丘脑最低（29.6±12.8 fmol/mg蛋白质）。此外，观察到[3H]LTB4和[3H]LTE4存在较弱的低容量结合，而[3H]LTD4未观察到可饱和结合。抑制[3H]LTC4结合的选择性顺序为LTC4远大于LTD4 = LTE4大于LTB4。
