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首页> 外文期刊>Biochimica et biophysica acta: international journal of biochemistry and biophysics >Identification of carbohydrate deficient transferrin forms by MALDI-TOF mass spectrometry and lectin ELISABiochim Biophys Acta 1998 Aug 24;1381(3):356
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Identification of carbohydrate deficient transferrin forms by MALDI-TOF mass spectrometry and lectin ELISABiochim Biophys Acta 1998 Aug 24;1381(3):356

机译:通过MALDI-TOF质谱和凝集素ELISA鉴定碳水化合物缺乏的转铁蛋白形式Biochim Biophys Acta 1998年8月24日; 1381(3):356

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摘要

Transferrin was isolated from sera of patients with severe alcohol abuse and from control sera by affinity chromatography using an immobilized polyclonal antibody from sheep, followed by gel filtration. The purified transferrin was then separated by MonoQ chromatography. Compared to the controls, sera from heavy alcohol consumers showed two additional transferrin peaks, eluting earlier than the three main transferrin forms present in all sera. Further analysis of the isolated transferrin forms by matrix assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) and enzyme linked immunosorbent assay with different digoxigenylated lectins (lectin ELISA) revealed that the main carbohydrate deficient transferrin (CDT) forms are lacking either one or both of the N-Glycan chains.
机译:通过使用绵羊固定化多克隆抗体的亲和层析,从重度酒精滥用患者的血清和对照血清中分离转铁蛋白,然后进行凝胶过滤。然后通过MonoQ色谱分离纯化的转铁蛋白。与对照相比,来自重度饮酒者的血清显示了两个额外的转铁蛋白峰,比所有血清中存在的三种主要转铁蛋白形式更早洗脱。通过基质辅助激光解吸/电离飞行时间质谱(MALDI-TOF-MS)和酶联免疫吸附测定法(使用不同的地高辛烯化的凝集素(凝集素ELISA))对分离的转铁蛋白形式进行进一步分析,发现主要的碳水化合物缺陷型转铁蛋白(CDT)形式缺少一个或两个N-糖链。

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