Future Prospects for the Use of Monoclonal Antibodies Research Paper

Future Prospects for the Use of Monoclonal Antibodies - Research Paper ExampleLater, Behring suggested that active immunity could be produced in humans by a combination of diphtheria toxin and antitoxin serum (Llewelyn, Hawkins, Russell, 1992). However, it was Paul Ehrlich whose work made it doable to produce antiserum to diphtheria toxin on a mass scale. The side chain theory of toxicity was proposed by Ehrlich, match to which, toxins mediated their effects on cells through preformed protein side bonds and immunity arose because of overproduction of these side chains (Llewelyn, Hawkins, Russell, 1992.) Csar Milstein and Georges Khler, in 1975, managed to produce in vitro custom-built antibodies. They produced a hybridoma by fusing rodent antibody-producing cells with neoplasm cells from mice bone marrow. A hybridoma, provided with the correct nutrients, can grow indefinitely and divide to produce monoclonal antibodies (antibodies of a angiotensin-converting enzyme type), on a la rge scale (Saldanha, 2000.) Five classes of immunoglobulin (Ig) are found in mammals IgA, IgD, IgE, IgG, and IgM. In some select mammals, IgG and IgA are further subdivided into subclasses (isotypes) due to polymorphisms in the doughy chain (Lipman et al, 2005). The prototype antibody is IgG, which is a glycoprotein having a molecular weight of 150000 Dalton. The molecule has a Y shape structure, consisting of two identical knockout chain-light chain heterodimers, that is linked together by a disulfide bridge. While the heavy chain comprises three constant immunoglobulins (Ig) domains and one variable (V) domain, the light chains consist of a single constant Ig domain and a single variable domain. The host defense mechanism is initiated by the antigen binding site (Fab) and the Fc region (fragment crystallizable) site (Llewelyn, Hawkins, Russell, 1992.) In order to effectively bind a large range of antigens, there are numerous mechanisms which come into play.