31
Oct
Structure Of Igg And Igm. The hinge region is the area of the H chains between the first and second C region domains and is held together by disulfide bonds. It takes 100 to 1000 times more molecules of IgG than of IgM to achieve the same level of agglutination. The four chains are covalently bonded together by disulfide bonds. The molecular weight of IgM is 900000MW or 900kDa and that of IgG is 150000MW or 150kDa.
IgM is a better agglutinin than other antibody isotypes. This is the key difference between IgM and IgG. STRUCTURE AND SOME PROPERTIES OF IG CLASSES AND SUBCLASSES. This flexible hinge found in IgG IgA and IgD but not IgM or IgE region allows the distance between the two antigen-binding sites to vary. IgM account only 10 of the total volume of the serum and IgG occupies 75 of the total volume of the serum. Antibody molecules of type IgG are composed of four polypeptide chains two identical copies of each a light chain L and heavy chain H.
The subclasses differ in the number of disulfide bonds and length of the hinge region.
The hinge region is the area of the H chains between the first and second C region domains and is held together by disulfide bonds. This is the key difference between IgM and IgG. Immunoglobulin G IgG the most abundant type of antibody is found in all body fluids and protects against bacterial and viral infections. IgM is a better agglutinin than other antibody isotypes. It has a molecular weight of 900000 Daltons. Because of its large size 900 kDa IgM is found primarily in the intravascular space.