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首页> 外文期刊>Neurochemistry International: The International Journal for the Rapid Publication of Critical Reviews, Preliminary and Original Research Communications in Neurochemistry >Chemical modification of the dihydropyridines binding sites by lysine reagent, pyridoxal 5'-phosphate.
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Chemical modification of the dihydropyridines binding sites by lysine reagent, pyridoxal 5'-phosphate.

机译：通过赖氨酸试剂吡ido醛5'-磷酸对二氢吡啶结合位点进行化学修饰。

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摘要

Treatment of rabbit brain membranes of the DHP binding sites of L-type Ca2+ channel with lysine-specific reagent resulted in a time- and concentration-dependent loss of [3H]nitrendipine binding activity. Following exposure to the maximum concentration of PLP (100 mM), [3H]nitrendipine binding was inhibited by up to 96.5%. Scatchard analysis of the binding data indicated that treatment with PLP resulted in a loss of [3H]nitrendipine binding sites with no effect on binding affinity. Considerable protection against PLP inactivation was obtained by nifedipine. These results indicate that lysine residue plays a critical role in maintaining the DHP-binding sites in a conformation capable of ligand binding.
机译：用赖氨酸特异性试剂处理兔脑膜L型Ca2 +通道的DHP结合位点会导致[3H]硝苯地平结合活性的时间和浓度依赖性丧失。暴露于最大浓度的PLP（100 mM）后，[3H]硝苯地平的结合被抑制了多达96.5％。对结合数据的Scatchard分析表明，用PLP处理导致[3 H]硝苯地平结合位点的损失，而对结合亲和力没有影响。硝苯地平可有效防止PLP失活。这些结果表明赖氨酸残基在维持DHP结合位点处于能够与配体结合的构象中起关键作用。

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