|Title||Glycoprotein analysis using mass spectrometry: unraveling the layers of complexity.|
|Publication Type||Journal Article|
|Year of Publication||2012|
|Journal||Anal Bioanal Chem|
|Date Published||2012 Sep|
|Keywords||Amino Acid Sequence, Animals, Glycoproteins, Glycosylation, Humans, Mass Spectrometry, Molecular Sequence Data|
A glycoprotein exists as a heterogeneous mixture of forms due to differential glycosylation, each of which may confer different functionality and/or serve as a biochemical marker for disease. The complex structure of glycans make them a bioanalytical challenge requiring multiple mass spectrometry based approaches to gain different types of information. The following article will briefly describe recently utilized mass spectrometry methods to identify glycosylation sites and measure glycan composition, sequence, branching, and relative quantities. Potential metrological developments are discussed in light of current trends toward complete, reliable glycoanalytical characterization in a high-throughput manner.
|Alternate Journal||Anal Bioanal Chem|