Kinniburgh D W, Boyd N D
Clin Pharmacol Ther. 1981 Feb;29(2):203-10. doi: 10.1038/clpt.1981.32.
Drug binding to protein is known to be altered in renal disease. Explanations include hypoproteinemia, competitive or noncompetitive inhibition, and basic functional defects in the binding protein. Albumin, the primary binding protein for phenytoin (DPH), was isolated from the plasma of patients with severe renal failure as well as from normal controls. DPH binding was not different between the albumin preparations isolated from the two sources, although some differences were detected in the apparent affinity constant and the number of binding sites. It would appear that the significant defect in DPH binding in renal disease cannot be attributed to a basic functional defect in the drug-binding protein albumin.
已知药物与蛋白质的结合在肾脏疾病中会发生改变。其原因包括低蛋白血症、竞争性或非竞争性抑制以及结合蛋白的基本功能缺陷。白蛋白是苯妥英钠（DPH）的主要结合蛋白，从严重肾衰竭患者的血浆以及正常对照者的血浆中分离得到。尽管在表观亲和常数和结合位点数量上检测到了一些差异，但从这两种来源分离得到的白蛋白制剂之间的DPH结合并无差异。看来，肾脏疾病中DPH结合的显著缺陷不能归因于药物结合蛋白白蛋白的基本功能缺陷。
