Snapshots in the history of Immunoglobulin molecules
Porter digested γ-globulins with papain, a proteolytic enzyme, and recovered 3 fractions: Fractions I and II of molecular weights between 50 and 55KDa retained the antigen binding capacity, whereas fraction III, of 80 KDa was crystalizable, and have a higher carbohydrate content (Porter RR, Biochem J. 73:119-127, 1959).
Heavy and Light chains
Edelman and Poulik reported that rabbit 7S γ-globulins and human myeloma proteins reduced in strong urea solutions and alkylated, separated into heavy (H) and light (L) chains bound by disulfide bonds (Edelman GM and Poulik MD, J Exp Med. 113:861-884, 1961)
Porter and colleagues proposed the basic Y structure of four polypeptide chains and 5 interchain disulfide bonds (Fleischman JB et al., Biochem J. 88:220-228, 1963)
Tomasi and coworkers demonstrated that IgA present in saliva and colostrum is produced locally and secreted as a dimer or trimer by (Tomasi TB et al., J Exp Med 121:101-124, 1965) and Newcomb and coworkers demonstrated the existence of the secretory piece (Newcomb RW et al., J immunol 101:905-913, 1968).
Variable and Constant Regions
Edelman and coworkers reported the first complete sequence of a γG immunoglobulin molecule and demonstrated the existence of variable (V) and constant (C) regions in the H and L chains (Edelman GM et al., Proc Nat Acad Sci USA 63:78-85, 1969)
Koshland and coworkers demonstrated that the monomers of the polymeric IgM and IgA are linked by the J chain in a clasp way (Halpern MS and Koshland ME. Nature 228:1276-1278, 1970; Chapuis RM, Koshland ME, Proc Nat Acad Sci 71:657-661, 1974)
Poljak and colleagues described the three-dimensional structure of IgG(l) myeloma protein (Poljak et al., Proc Nat Acad Sci 71. 3440-3444, 1974).
History kindly supplied by Dr Luis Garcia – Immunopaedia Steering Committee