Interference No. 102,572
monomers are linked by disulfide bonds to form the basic dimeric structure of the molecule
(Cabilly et al. specification, page 5). There are five classes or types of H chains, gamma,
mu, alpha, delta, or epsilon which characterize an individual Ig as an IgG, IgM, IgA, IgD or
IgE, respectively; and two classes of L chains, kappa (6) and lambda (8) (Cabilly et al.
specification, page 5). Each antibody chain contains a variable region (V) and a constant
region. The variable region is about 100 amino acids in length and is specific for the
antigen which elicited it. (Cabilly et al. specification, page 6). The constant region does
not take part in the binding of any antigenic determinant but does serve to link the antibody
to other participants in the immune defenses, e.g. to fix complement, and thus makes an
antibody bifunctional. The variable region of the H and L chain interact closely and when
correctly folded form a three dimensional site at each branch of the Y for binding to a
particular portion or epitope of the specific antigen which elicited the antibody(Cabilly et al.
specification, page 5-6, and Boss et al. patent, column 1, line 60-column 2, line 47).
Kohler and Milstein developed a technique that made it possible to produce
monoclonal antibodies, i.e., homogenous antibodies of a single class and single
specificity, by the use of hybridoma technology. Monoclonal antibodies are produced in
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