Site-Specific Quantitative Evaluation of the Protein Glycation ProductN6-(2,3-Dihydroxy-5,6-dioxohexyl)-l-lysinate by LC−(ESI)MS Peptide Mapping:  Evidence for Its Key Role in AGE Formation

2003 ◽  
Vol 14 (3) ◽  
pp. 619-628 ◽  
Author(s):  
Klaus M. Biemel ◽  
Markus O. Lederer
Keyword(s):  
Quantitative Evaluation ◽  
Peptide Mapping ◽  
Protein Glycation ◽  
Site Specific ◽  
Esi Ms

scholarly journals Quantitative evaluation of noncovalent chorismate mutase-inhibitor binding by ESI-MS

2003 ◽  
Vol 14 (12) ◽  
pp. 1470-1476 ◽  
Author(s):  
Silke Wendt ◽  
Gregor McCombie ◽  
Jürg Daniel ◽  
Alexander Kienhöfer ◽  
Donald Hilvert ◽  
...  
Keyword(s):  
Quantitative Evaluation ◽  
Chorismate Mutase ◽  
Inhibitor Binding ◽  
Esi Ms

Site-specific characterisation of densely O-glycosylated mucin-type peptides using electron transfer dissociation ESI-MS/MS

2011 ◽  
Vol 32 (24) ◽  
pp. 3536-3545 ◽  
Author(s):  
Morten Thaysen-Andersen ◽  
Brendan L. Wilkinson ◽  
Richard J. Payne ◽  
Nicolle H. Packer
Keyword(s):  
Electron Transfer ◽  
Electron Transfer Dissociation ◽  
Site Specific ◽  
Esi Ms

A quantitative evaluation of ten approaches to setting site‐specific cleanup objectives

1992 ◽  
Vol 1 (1) ◽  
pp. 39-59 ◽  
Author(s):  
Barry Jessiman ◽  
G. Mark Richardson ◽  
Cathy Clark ◽  
Bruce Halbert
Keyword(s):  
Quantitative Evaluation ◽  
Site Specific

scholarly journals Glycoproteomic measurement of site-specific polysialylation

2019 ◽  
Author(s):  
Ruby Pelingon ◽  
Cassandra L. Pegg ◽  
Lucia F. Zacchi ◽  
Toan K. Phung ◽  
Christopher B. Howard ◽  
...  
Keyword(s):  
Protein Function ◽  
Neurological Diseases ◽  
Polysialic Acid ◽  
Monosaccharide Composition ◽  
Degree Of Polymerization ◽  
Site Specific ◽  
Esi Ms ◽  
Therapeutic Drugs ◽  
Protease Digestion ◽  
Analytical Approaches

AbstractPolysialylation is the enzymatic addition of a highly negatively charged sialic acid polymer to the non-reducing termini of glycans. Polysialylation plays an important role in development, and is involved in neurological diseases, neural tissue regeneration, and cancer. Polysialic acid (PSA) is also a biodegradable and non-immunogenic conjugate to therapeutic drugs to improve their pharmacokinetics. PSA chains vary in length, composition, and linkages, while the specific sites of polysialylation are important determinants of protein function. However, PSA is difficult to analyse by mass spectrometry (MS) due to its high negative charge and size. Most analytical approaches for analysis of PSA measure its degree of polymerization and monosaccharide composition, but do not address the key questions of site specificity and occupancy. Here, we developed a high-throughput LC-ESI-MS/MS glycoproteomics method to measure site-specific polysialylation of glycoproteins. This method measures site-specific PSA modification by using mild acid hydrolysis to eliminate PSA and sialic acids while leaving the glycan backbone intact, together with protease digestion followed by LC-ESI-MS/MS glycopeptide detection. PSA-modified glycopeptides are not detectable by LC-ESI-MS/MS, but become detectable after desialylation, allowing measurement of site-specific PSA occupancy. This method is an efficient analytical workflow for the study of glycoprotein polysialylation in biological and therapeutic settings.Graphical Abstract

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