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首页> 外文期刊>Journal of Agricultural and Food Chemistry >Increase of Ovalbumin Glycation by the Maillard Reaction after Disruption of the Disulfide Bridge Evaluated by Liquid Chromatography and High Resolution Mass Spectrometry
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Increase of Ovalbumin Glycation by the Maillard Reaction after Disruption of the Disulfide Bridge Evaluated by Liquid Chromatography and High Resolution Mass Spectrometry

机译：通过液相色谱和高分辨率质谱评估二硫键断裂后美拉德反应引起的卵清蛋白糖基化增加

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摘要

The number of glycation sites of ovalbumin was monitored by Fourier transform ion cyclotron mass spectrometry (FTICR-MS) before and after reducing the pair of the intrachain disulfide bond. Reducing the disulfide bond of the protein greatly improved the reactivity of glycation both in dry-state and solution. The glycation sites identified by MS/MS showed that the major glycation sites of the ovalbumin were lysines. Our results suggest that glycation is strongly dependent on the protein tertiary structure, with significantly stronger reaction when the protein tertiary structure is disrupted after reducing the disulfide bond. The number,of glycated sites of the protein was increased from seven to twelve in dry-state and one to two in aqueous solution. The glycation sites were found to be regulated by protein tertiary structure, hydrogen bonding, and neighboring amino acid compositions.
机译：在还原一对链内二硫键之前和之后，通过傅立叶变换离子回旋加速器质谱（FTICR-MS）监测卵清蛋白糖基化位点的数目。减少蛋白质的二硫键，可大大改善干态和溶液中糖基化的反应性。 MS / MS鉴定的糖基化位点表明卵清蛋白的主要糖基化位点是赖氨酸。我们的结果表明，糖基化强烈依赖于蛋白质的三级结构，当还原二硫键后破坏蛋白质的三级结构时，其糖化反应明显增强。蛋白质的糖基化位点数在干燥状态下从7个增加到12个，在水溶液中从1个增加到2个。发现糖基化位点受蛋白质三级结构，氢键和邻近氨基酸组成的调节。

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