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heavy chains (H) in the so-called Fc fragments (crystallizable fragments) determines the antibody class: the most abundant classes are called IgG, IgM, IgA, IgE, and IgD. Antibodies in different classes may have exactly the same antigenbinding properties, but exhibit different functional properties. The abundances and functional properties of the ve major classes of antibodies3 are listed in Table 5.1. Antiserum is that part of the serum containing antibodies. It may be prepared from whole serum by a series of ammonium sulfate precipitation steps, where successively lower concentrations of ammonium sulfate generate a precipitate that is centrifuged and resuspended in buffer.4 The antiserum is then dialized or af nitypuri ed, and assayed for total protein. The selectivity of antigen antibody (and hapten antibody) interactions is analogous to the selectivity of substrate enzyme interactions. The antigen-binding site of an antibody has a structure that allows a complementary t with structural elements and functional groups on the antigen. The portion of the antigen that interacts speci cally with the antigen-binding site on the antibody is called the antigenic determinant, or epitope. The epitope has a size of $ 0:7 1:2 3:5 nm, which is equivalent to $ 5 7 amino acid residues. The complementary site on the antibody is called the paratope, and this has about the same size. Antigens may be classi ed according to their binding characteristics of valency (meaning the total number of sites) and their determinacy (meaning the number of different types of sites).5 There are four classes of antigens: 1. Only a single epitope on the surface that is capable of binding to an antibody: unideterminate and univalent. Haptens are unideterminate and univalent. 2. Two or more epitopes of the same kind on one antigen molecule: unideterminate and multivalent. 3. Many epitopes of different kinds, but only one of each kind on one antigen molecule: multideterminate and univalent. Most protein antigens fall into this category. 4. Many epitopes of different kinds, and more than one of each kind per antigen molecule: multideterminate and multivalent. Proteins containing multiple identical subunits, as well as polymerized proteins and whole cells, fall into this category.
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Binding interactions between antigen and antibody involve electrostatic, hydrophobic, and van der Waals interactions, as well as hydrogen bonding. These are all relatively weak, noncovalent forces, and for this reason, complementarity must extend over a relatively large area to allow the summation of all available interactions. Antigen antibody association constants are often as high as 1010 M 1 . 5.3. POLYCLONAL AND MONOCLONAL ANTIBODIES Polyclonal antibodies are isolated directly from serum, by a similar procedure to the one outlined earlier in this chapter. The immunogen used to generate polyclonal antibodies may consist of a small molecule (a hapten) covalently bound to a carrier protein. The resulting antiserum will contain a mixture of antibodies that bind to different epitopes of the hapten carrier conjugate, as well as antibodies generated in response to other immunogens present in the organism. This results in an antiserum possessing a wide range of selectivities and af nities, and may result in signi cant cross-reactivities, or interferences, when employed in immunoassays. Monoclonal antibodies6 are a homogeneous population of identical antibody molecules, having identical paratopes and af nity for a single antigenic epitope. They are biochemically synthesized in a procedure rst described by Milstein and Kohler in the 1970s, work for which these researchers won the Nobel Prize.
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Figure 5.3. The generation of hybridoma cell lines for monoclonal antibody production.
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Figure 5.3 shows an outline of Milstein and Kohler s procedure for monoclonal antibody production. An animal immunized with an antigen (Ag) increases its population of antibody (Ab)- producing lymphocytes. These cells are short lived and can exist in cell cultures only for a few days. Malignant plasma cells are separately cultured. These cells are essentially immortal, and can be cultured for years, but they are poor producers of Abs. Some malignant plasma cells are de cient in the enzyme hypoxanthine phosphoribosyltransferase (HPRT), and will die unless HPRT is supplied to the culture medium. These are the malignant cells that are used for the production of hybridomas. Hybridomas (or fused cell culture lines) are produced by fusing lymphocytes isolated from the spleen of an immunized animal with the HPRT de cient malignant plasma cells. The lymphocytes. The unfused cells die, since spleen cells survive only a few days, while the malignant plasma cells lack HPRT. Fused cells, however, are HPRT positive as well as immortal; these hybridomas, or hybrid cells, retain the Ab-producing characteristics of the spleen cells. Hybrid cell lines that produce a speci c antibody are then cloned from the single cells and cultured. Each clone created in this manner produces antibodies of a single epitope speci city! While monoclonal antibodies are initially almost prohibitively expensive to produce, they offer very distinct advantages over polyclonal antisera for analytical applications. Of primary importance is the immortality of the hybridoma lines: monoclonal Abs produced by this cell line will show relatively little batch-tobatch variation, and the repetitive use of animals for antibody production becomes unnecessary. In addition, the single-epitope selectivity of the monoclonal Ab tends to minimize cross-reactions, except with epitopes possessing very similar structural characteristics to the original antigen s epitope. 5.4. ANTIBODY ANTIGEN INTERACTIONS The interactions of antibodies with their selective binding partners, antigens or haptens, are classi ed as primary or secondary binding interactions. Primary interactions involve the speci c recognition and combination of an antigenic determinant (epitope) with the binding site (paratope) of its corresponding antibody. All Ab Ag interactions begin with a primary interaction, which occurs very rapidly (on a millisecond time scale), and is macroscopically invisible. The equilibrium relationships involved in the primary binding interaction can be studied using haptens, which, due to their univalent, unideterminate nature, prevent secondary binding interactions from occurring. Free hapten exists in equilibrium with antibody-bound hapten as shown below (Eq. 5.1):
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