The deglycosylation rate can be increased by denaturation of the glycoproteins (e.g., by carboxymethylation, sulfitolysis or by heating in the presence of sodium dodecyl sulfate).
Most proteins destined for the cell surface are translated by ribosomes into the rough endoplasmic reticulum (ER) and translocated into the Golgi.
Upon entering the ER a molecule containing 14 sugar subunits is linked en bloc to an asparagine in a selective manner by the enzyme oligosaccharyl transferase.
It is this oligosaccharide molecule which is modified by a series of enzymes as the protein moves through the different compartments of the Golgi apparatus.
Endoglycosidase H is able to cleave each structure of this oligosaccharide as it is processed until the enzyme Golgi α-mannosidase II removes two mannose subunits.