BINDING OF SULFONYLUREAS TO SERUM-ALBUMIN
BINDING OF SULFONYLUREAS TO SERUM-ALBUMIN
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DOI：
10.1111/j.2042-7158.1974.tb09280.x
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发表时间：
1974-01-01
影响因子：
3.3
通讯作者：
BROWN, KF
中科院分区：
文献类型：
--
作者：
CROOKS, MJ;BROWN, KF
研究了甲苯磺丁脲、格列本脲、氯磺丙脲和妥拉磺脲与血清白蛋白的相互作用。格列本脲是四种化合物中结合力最强的，仅与一类位点结合。其他三种化合物与至少两种化合物结合。格列本脲和白蛋白之间的相互作用是独立的pH值和温度降低显着增加，表明一个非离子机制参与。与此相反，甲苯磺丁脲与白蛋白的整体相互作用表现出很小的温度依赖性，此外，结合甲苯磺丁脲和氯磺丙脲的pH值下降。这些研究结果意味着，主要结合的物种是阴离子。结合静电效应校正参数被认为是适合结合数据甲苯磺丁脲，氯磺丙脲和甲磺脲比未校正的参数。格列本脲结合的静电校正是不必要的。
The interaction of tolbutamide, glibenclamide, chlorpropamide and tolazamide with serum albumin has been examined. Glibenclamide, the most strongly bound of the four compounds, is bound to only one class of sites. The other three compounds are bound to at least two. The interaction between glibenclamide and albumin was independent of pH and increased markedly with decreasing temperature suggesting that a non-ionic mechanism is involved. In contrast, the overall interaction of tolbutamide with albumin showed little temperature dependence and, in addition, binding of both tolbutamide and chlorpropamide decreased with pH. These findings imply that the predominantly bound species is the anion. Binding parameters corrected for electrostatic effects were found to fit binding data for tolbutamide, chlorpropamide and tolazamide better than uncorrected parameters. Electrostatic correction of binding of glibenclamide is unnecessary.