Immunoglobulins are used by the immune system present in serum and tissue fluids to identify and neutralize foreign targets. Immunoglobulins are “Y”-shaped molecules comprised of two identical light chains (L) and two identical heavy chains (H) linked via disulfide covalent forces and via non-covalent interactions. Each chain has constant (CL and CH) and variable (VL and VH) domains (Holt et al. 2003). These form two antigen-binding fragments (Fab) that specifically recognize and bind to antigen molecule and a constant fragment (Fc) which is responsible for the effector function and biodistribution of the antibody (Beale 1987). Proteolytic digestion provides important information to determine an antibody molecule’s structure and function. Antibody molecules can be cleaved into fragments and each of these fragments has a distinct activity. A number of enzymes like papain, pepsin, ficin, bromelain, and elastase can be used for this purpose, papain being the most frequently used (Luo et...
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Bereli, N., Yavuz, H., Denizli, A. (2016). Affinity Separation and Crystallization of Fc Fragments. In: Drioli, E., Giorno, L. (eds) Encyclopedia of Membranes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-44324-8_690
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