Post-translational non-enzymatic modification of proteins. II. Separation of selected protein species after glycation and other carbonyl-mediated modifications.

作者: Ivan Mikšík , Zdeněk Deyl

DOI: 10.1016/S0378-4347(97)00233-8

关键词: GlycationGel permeation chromatographyChromatofocusingGel electrophoresisPentosidineChemistryLens proteinSize-exclusion chromatographyGlycosylationBiochemistryChromatography

摘要: There are two strategies applicable to revealing non-enzymatic post-translational modifications of proteins; while assaying the hydrolytically stable adducts was subject our previous communication [1], here we attempted review separation technologies for unfragmented modified proteins. a few standard procedures used this purpose, namely Laemmli gel electrophoresis, different modes permeation chromatography and boronate affinity chromatography. The latter approach makes use vicinal hydroxy groups present in glycated Some (but not all) arising exhibit typical fluorescence which can be exploited detection. In most cases is measured at 370/440 nm so-called advanced glycation products or 335/385 only so far well characterized marker (pentosidine). indication exists that, e.g., synchronous detection will probably future add selectivity allow distinction during (glycation). proteins reviewed serum albumin, collagen lens hemoglobin another within volume.

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