Treatment of IgG with papain produces how many fragments from each immunoglobulin molecule?

When IgG is treated with the proteolytic enzyme papain, the molecule is cleaved into three distinct fragments. Papain hydrolyzes the disulfide bonds that link the heavy chains of the antibody, leading to the formation of two Fab (fragment antigen-binding) regions and one Fc (fragment crystallizable) region.

The two Fab fragments are responsible for binding to antigens, while the Fc fragment plays a key role in mediating interactions with various components of the immune system, such as complement proteins and Fc receptors on immune cells. This cleavage produces a total of three fragments from each IgG molecule: two that can bind antigen and one that interacts with immune system components, accounting for the total of three fragments resulting from papain treatment.

Understanding the process and outcomes of such proteolytic treatments is important not only for their immunological implications but also their applications in diagnostics and therapeutic development.