Location of Specificity and Allotypic Amino Acid Residues in Antibody Fd Fragments
This extract was created in the absence of an abstract.
Excerpt
Because of both the heterogeneity and limited supply of purified antibody, structural studies have been carried out on the homogeneous myeloma proteins which may belong to any one of the major classes of immunoglobulins but which lack antibody activity. Comparative analyses of human myeloma light chains by Putnam and Easley (1965), Hilschmann and Craig (1965), Titani, Whitley, Avogardo, and Putnam (1965), and Milstein (1966), and of mouse light chains by Hood, Gray, and Dreyer (1966) have provided the dramatic result of an amino-terminal half of variable sequence and a carboxy-terminal half of nearly invariant sequence. A similar structure appears likely for the heavy chain from the amino-terminal analyses of Wilkinson, Press, and Porter (1966) and the sequence determination of the common carboxyterminal portion by Hill, Delaney, Lebovitz, and Fellows (1966).
On the basis of these studies antibody activity has been identified with the variable region. It seemed logical that the...
