Final answer:
Disulfide bonds on antibodies are typically between the light and heavy chains, linking their variable and constant domains. These bonds play a key role in maintaining the structure and function of the antibody molecule.
Step-by-step explanation:
Disulfide bonds in antibodies are crucial for the structural integrity of these immunoglobulins. These bonds are found between different domains of the antibody molecule. The correct answer to the question 'Disulfide bonds on antibodies are between which domains?' is b) Light and Heavy. The light and heavy chains in antibodies are linked together by disulfide bonds. More specifically, these bonds occur both within the light and heavy chains, stabilizing their individual structures, and between the light and heavy chains, contributing to the overall structural stability of the antibody molecule.
Each light chain contains one variable (v) domain and one constant (c) domain, while each heavy chain contains one variable domain and three or four constant domains, depending on the antibody class. The Fab region of an antibody consists of both light and heavy chain variable domains that bind to antigens, whereas the Fc region is constituted by the constant domains of the heavy chains and is responsible for mediating immune effector functions.