首页> 外文期刊>Life sciences >Glycation of human serum albumin by acylglucuronides of nonsteroidal anti-inflammatory drugs of the series of phenylpropionates.
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Glycation of human serum albumin by acylglucuronides of nonsteroidal anti-inflammatory drugs of the series of phenylpropionates.

机译:系列苯丙酸酯类非甾体类抗炎药的酰基葡糖醛酸糖苷对人血清白蛋白的糖基化作用。

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摘要

The covalent binding to human serum albumin (HSA), of acylglucuronides from carboxylic nonsteroidal anti-inflammatory drugs (NSAIDs) was investigated. The adduct formation was followed and quantitated by HPLC and by radiometric detection. Three types of albumin adducts were evidenced. The acylglucuronide or the drug itself was bound to 0.2 up to 9% of the albumin molecules, depending on the drug, whereas the majority of adducts (23-49% of albumin molecules) retained the glucuronic acid moiety. The possible involvement of specific Lys located in site I of albumin in the formation of these main adducts was demonstrated, using a series of HSA whose specific Lys residues have been modified chemically. This study shows that acylglucuronides from NSAIDs can significantly contribute to the glycation of proteins, such as albumin.
机译:研究了来自羧基非甾体抗炎药(NSAID)的酰基葡糖醛酸苷与人血清白蛋白(HSA)的共价结合。跟踪加合物的形成,并通过HPLC和放射检测定量。证实了三种类型的白蛋白加合物。取决于药物,酰基葡糖醛酸或药物本身结合至0.2至9%的白蛋白分子,而大多数加合物(占白蛋白分子的23-49%)保留了葡萄糖醛酸部分。使用一系列HSA,其特定的Lys残基已经过化学修饰,证明了位于白蛋白I位点的特定Lys可能参与了这些主要加合物的形成。这项研究表明,来自NSAID的酰基葡糖醛酸能显着促进蛋白质(如白蛋白)的糖基化。

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