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- W1513826044 abstract "Mass spectrometry has become one of the methods of choice in uncovering many important post-translational changes in proteins, for it is capable of revealing the presence and nature of modifications, as well as locating which amino acid has been modified. This chapter describes studies on protein glycosylation and phosphorylation, and illustrates a preliminary evaluation of the stepped collision energy LC-ESMS method for selective detection of sulfated and acylated peptides in protein digest. The chapter proposes to find neuraminidase treatment to be helpful in reducing glycopeptides heterogeneity somewhat, and in enhancing the MS detection of glycopeptides. Microheterogeneity within the glycopeptide due to differences in glycosylation has a small, but noticeable influence on the elution times on C18 reverse-phase chromatography. It is also shown that having isolated, the phosphopeptide-containing fractions, it becomes possible to try to locate the site of phosphorylation by tandem mass spectrometry. Fatty acylation of proteins is a common post-translational modification that blocks sequencing of the N-terminal amino acids by Edman techniques. Mass spectrometry can play an essential role in such sequencing; however, it is not always trivial to locate the blocked N-terminal peptide. The chapter discusses that phosphopeptides and sulfopeptides can be distinguished in a single experiment." @default.
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- W1513826044 date "1995-01-01" @default.
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- W1513826044 title "LC-MS methods for selective detection of posttranslational modifications in proteins: Glycosylation, phosphorylation, sulfation, and acylation" @default.
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- W1513826044 doi "https://doi.org/10.1016/s1080-8914(06)80016-5" @default.
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