Editing Glycoprotein (section)

== Analysis ==
A variety of methods used in detection, purification, and structural analysis of glycoproteins are<ref name="Murray" />{{rp|525}}<ref name="immune_glycan"/><ref name="Dell_2001" />

{| class="wikitable"
|+Some important methods used to study glycoproteins
|-
! Method
! Use
|-
| [[Periodic acid-Schiff stain]]
| Detects glycoproteins as pink bands after [[Electrophoresis|electrophoretic]] separation.
|-
| Incubation of cultured cells with glycoproteins as [[radioactive decay]] bands
| Leads to detection of a radioactive sugar after electrophoretic separation.
|-
| Treatment with appropriate [[Endoglycosidase|endo-]] or [[exoglycosidase]] or [[phospholipase]]s
| Resultant shifts in electrophoretic migration help distinguish among proteins with N-glycan, O-glycan, or GPI linkages and also between high [[mannose]] and complex N-glycans.
|-
| [[Agarose]]-[[lectin]] [[column chromatography]], [[lectin affinity chromatography]]
| To purify glycoproteins or glycopeptides that bind the particular lectin used.
|-
| [[Lectin]] [[affinity electrophoresis]]
| Resultant shifts in electrophoretic migration help distinguish and characterize [[glycoform]]s, i.e. variants of a glycoprotein differing in carbohydrate.
|-
| Compositional analysis following acid [[hydrolysis]]
| Identifies sugars that the glycoprotein contains and their stoichiometry.
|-
| [[Mass spectrometry]]
| Provides information on [[molecular mass]], composition, sequence, and sometimes branching of a glycan chain. It can also be used for site-specific glycosylation profiling.<ref name = "immune_glycan"/>

|-
| [[NMR spectroscopy]]
| To identify specific sugars, their sequence, linkages, and the anomeric nature of glycosidic chain.
|-
| [[Multi-angle light scattering]]
| In conjunction with size-exclusion chromatography, UV/Vis absorption and differential refractometry, provides information on [[molecular mass]], protein-carbohydrate ratio, aggregation state, size, and sometimes branching of a glycan chain. In conjunction with composition-gradient analysis, analyzes self- and hetero-association to determine binding affinity and stoichiometry with proteins or carbohydrates in solution without labeling.
|-
| [[Dual Polarisation Interferometry]]
|  Measures the mechanisms underlying the biomolecular interactions, including reaction rates, affinities and associated [[conformational change]]s.
|-
| [[Methylation]] (linkage) analysis
| To determine linkage between sugars.
|-
| [[Amino acid]] or [[Complementary DNA|cDNA]] sequencing
| Determination of amino acid sequence.
|-
|}