Domingo M T, Spinnewyn B, Chabrier P E, Braquet P
Institut Henri Beaufour, Les Ulis, France.
Biochem Biophys Res Commun. 1988 Mar 15;151(2):730-6. doi: 10.1016/s0006-291x(88)80341-3.
The existence of specific binding sites for [3H]-labelled PAF ([3H]PAF) was investigated on membrane preparations of gerbil brain. Binding assays of [3H]PAF showed a specific, saturable, reversible and time dependent binding. Scatchard analysis indicated the presence of two apparent populations of binding sites with Kd1 = 3.66 +/- 0.92 nM and Kd2 = 20.4 +/- 0.50 nM corresponding respectively to a maximum number of binding sites: Bmax1 = 0.83 +/- 0.23 pmol/mg protein Bmax2 = 1.1 +/- 0.32 pmol/mg protein. The binding of [3H]PAF was fully displaced by unlabelled PAF and partially inhibited by the PAF antagonist BN 52021 suggesting that BN 52021 interacts only with one site. Distribution of [3H]PAF specific binding revealed a maximum amount of binding in midbrain and hippocampus. These data suggest a biochemical and physiological role of PAF in brain.
在沙鼠脑的膜制剂上研究了[3H]标记的血小板活化因子([3H]PAF)特异性结合位点的存在情况。[3H]PAF的结合试验显示出特异性、可饱和性、可逆性和时间依赖性结合。Scatchard分析表明存在两种明显的结合位点群体,其解离常数Kd1 = 3.66±0.92 nM,Kd2 = 20.4±0.50 nM,分别对应最大结合位点数:Bmax1 = 0.83±0.23 pmol/mg蛋白质,Bmax2 = 1.1±0.32 pmol/mg蛋白质。未标记的PAF可完全取代[3H]PAF的结合,而PAF拮抗剂BN 52021可部分抑制其结合,这表明BN 52021仅与一个位点相互作用。[3H]PAF特异性结合的分布显示中脑和海马中的结合量最大。这些数据表明PAF在脑中具有生化和生理作用。