describe the structure of antibody(4 marks
Answers
Explanation:
an antibody is a Y-shaped structure which consists of four polypeptides — two heavy chains and two light chains. This structure allows antibody molecules to carry out their dual functions: antigen binding and biological activity mediation.
Each function is carried out by different parts of the antibody: fragment antigen-binding (Fab fragment) and fragment crystallizable region (Fc region
Fab fragment is a region on an antibody that binds to antigens. It is composed of one constant and one variable domain of each of the heavy and the light chain. These domains shape the paratope — the antigen-binding site — at the amino terminal end of the monomer.
Fc region is the tail region of an antibody that interacts with cell surface receptors called Fc receptors and some proteins of the complement system. This property allows antibodies to activate the immune system. The Fc regions of immunoglobulin Gs bear a highly conserved N-glycosylation site.
Explanation:
Antibodies are glycoprotein which are highly specific to antigen. They are also known as immunoglobulin. They have 'Y' shaped structure. It consists of four polypeptide chain two heavy chains(H) and two light chains (L). The four polypeptide chain are hold together by disulfide bonds to form a Y shaped structure. The region holding arms and stem of antibody is termed as Hinge. Each chain of the antibody includes two distinct regions, the variable region and the constant region. Variable region constitute the antigen-binding site. This part of antibody recognized and binds to the specific antigen forming an antigen-antibody complex.
