228k views
4 votes
What is the result of enzymatic cleavage of the immunoglobulin monomer by pepsin?

a) Formation of two separate epitope-binding Fab fragments.
b) Disruption of interchain disulfide bonds.
c) Cleavage of the heavy-heavy chain disulfide bonds.
d) Formation of (Immunoreceptor) tyrosine activation motifs.
e) A molecule with two intact epitope-binding sites.

User Galgo
by
7.4k points

1 Answer

4 votes

Final answer:

The result of enzymatic cleavage of the immunoglobulin monomer by pepsin is A) the formation of two separate epitope-binding Fab fragments.

Step-by-step explanation:

When immunoglobulins are subjected to papain digestion, 3 fragments are produced. Two of these fragments retain the ability to bind with the antigen and are called antigen binding fragments (Fab). These Fab fragments have intact epitope-binding sites, allowing them to bind to antigens.

Therefore, the result of enzymatic cleavage of the immunoglobulin monomer by pepsin is the formation of two separate epitope-binding Fab fragments. The correct answer is A) the formation of two separate epitope-binding Fab fragments.

User Jadav Bheda
by
8.7k points