Institute of Physiology, Academy of Sciences of the Czech Republic, Vídeňská 1083, 142 20 Prague 4, Czech Republic.
J Chromatogr A. 2010 Dec 17;1217(51):8009-15. doi: 10.1016/j.chroma.2010.08.022. Epub 2010 Aug 13.
Non-enzymatic posttranslational modifications of bovine serum albumin (BSA) by various oxo-compounds (glucose, ribose, glyoxal and glutardialdehyde) have been investigated using high-performance liquid chromatography (HPLC) and capillary zone electrophoresis (CZE). Both of these methods used mass spectrometric (MS) detection. Three enzymes (trypsin, pepsin, proteinase K) were used to digest glycated BSA. The extent of modification depended on the selected oxo-compound. Reactivity increased progressively from glucose to glutardialdehyde (glucose<ribose<glyoxal<glutardialdehyde). Carboxymethylation of lysine (CML) was the main type of modification detected. The HPLC/MS method achieved higher coverage and a larger amount of CML was identified compared to CZE/MS.
使用高效液相色谱法（HPLC）和毛细管区带电泳法（CZE）研究了各种氧代化合物（葡萄糖、核糖、乙二醛和戊二醛）对牛血清白蛋白（BSA）的非酶翻译后修饰。这两种方法都使用质谱（MS）检测。三种酶（胰蛋白酶、胃蛋白酶、蛋白酶 K）用于消化糖化 BSA。修饰的程度取决于所选的氧代化合物。反应性从葡萄糖逐渐增加到戊二醛（葡萄糖<核糖<乙二醛<戊二醛）。检测到的主要修饰类型是赖氨酸的羧甲基化（CML）。与 CZE/MS 相比，HPLC/MS 方法实现了更高的覆盖率，并且鉴定出了更多的 CML。
