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Improving the Study of Protein Glycosylation with New Tools for Glycopeptide Enrichment

Title: Improving the Study of Protein Glycosylation with New Tools for Glycopeptide Enrichment
Authors: Samuelson, James C.
Contributors: Ruse, Cristian I.; Taron, Christopher H.; Ganatra, Mehul B.; Vainauskas, Saulius; McClung, Colleen M.; Dupard, Steven J.; Chen, Minyong
Source: MODID-6d55e02e354:IntechOpen
Publication Year: 2018
Subject Terms: Science / Life Sciences / Biochemistry; bisacsh:SCI007000
Description: High confidence methods are needed for determining the glycosylation profiles of complex biological samples as well as recombinant therapeutic proteins. A common glycan analysis workflow involves liberation of N-glycans from glycoproteins with PNGase F or O-glycans by hydrazinolysis prior to their analysis. This method is limited in that it does not permit determination of glycan attachment sites. Alternative proteomics-based workflows are emerging that utilize site-specific proteolysis to generate peptide mixtures followed by selective enrichment strategies to isolate glycopeptides. Methods designed for the analysis of complex samples can yield a comprehensive snapshot of individual glycans species, the site of attachment of each individual glycan and the identity of the respective protein in many cases. This chapter will highlight advancements in enzymes that digest glycoproteins into distinct fragments and new strategies to enrich specific glycopeptides.
Document Type: article in journal/newspaper
File Description: application/pdf
Language: English
Availability: https://openresearchlibrary.org/viewer/1e0d724d-1144-437c-aed1-fe23cc11f196; https://openresearchlibrary.org/ext/api/media/1e0d724d-1144-437c-aed1-fe23cc11f196/assets/external_content.pdf
Rights: https://creativecommons.org/licenses/by/4.0/legalcode
Accession Number: edsbas.F9EEA928
Database: BASE