作者: Joseph Zaia
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摘要: 1. ABSTRACT Structural variability resulting from protein post-translational glycosylation vastly increases the range of biological functions produced genome. The chemistry glycans differs that proteins and dictates use specialized mass spectrometric techniques for successful analysis. Moreover, unique each glycoconjugate class drives need tailored analytical techniques. Glycosaminoglycans (GAGs) are linear coat surfaces all animal cells, bound to syndecan glypican proteoglycan core proteins. There, they play developmentally critical roles as co-receptors many classes growth factors factor receptors. Animal cells grow in organized extracellular matrix environments consisting proteins, glycoproteins proteoglycans. GAGs serve create support immobilized gradients structural these matrices. Although, due their acidity, fragility polydispersity, have traditionally proven difficult analyze using spectrometry, effective new approaches emerged over past few years. This review summarizes biochemistry uses spectrometry analysis, with an emphasis on recent developments effective.