What method is used to release the N-linked glycan groups from the membrane-associated glycoconjugates shown in 1 in the figure below?
A) enzymatic cleavage using PNGaseF
B) chemical cleavage using a $\beta$-elimination reaction
C) chemical cleavage using a Schiff base intermediate
D) enzymatic cleavage using $\beta$-galactosidase

Question

What method is used to release the N-linked glycan groups from the membrane-associated glycoconjugates shown in 1 in the figure below? 
A) enzymatic cleavage using PNGaseF 
B) chemical cleavage using a $\beta$-elimination reaction 
C) chemical cleavage using a Schiff base intermediate 
D) enzymatic cleavage using $\beta$-galactosidase

Quizplus · Accepted Answer

Enzymatic cleavage using peptide N-glycosidase F (PNGaseF) is the most common and effective method for releasing N-linked glycan groups from glycoproteins. The enzyme cleaves the amide bond between the asparagine residue of the glycoprotein and the N-linked glycan. This results in the release of the glycan and the conversion of the asparagine residue to aspartic acid. Chemical cleavage using a F1F1F1S1βF1F1F10-elimination reaction or a Schiff base intermediate is not a common method to release N-linked glycans, and enzymatic cleavage using F1F1F1S1βF1F1F10-galactosidase is specific to removing galactose residues from the end of the glycan chain.

What Method Is Used to Release the N-Linked Glycan Groups β\betaβ

What Method Is Used to Release the N-Linked Glycan Groups $\beta$