Antigens interaction with homogeneous

Interaction of Homogeneous, Murine Myeloma Immunoglobulins with Polysaccharide Antigens, 31,313-346... 

Carbohydrates, Galactomannans. antigens, interaction of, with homogeneous, murine myeloma immunoglobulins, 31, 313-346 bibliography of crystal structures of, (1967-1974), 33, 387-404 (1975), 35, 377-385 noncytotoxic, antitumor, 32, 235-275 the pneumococcal, a re-examination of, 33, 295-322... 

Most of the agrochemicals are relatively small molecules and the antibodies produced in animals may, by comparison, be fairly uniform with respect to complementarity. When antisera to haptens are diluted sufficiently so as to favor interaction with the most avid antibodies, the Scatchard plots often are indicative of fairly homogeneous populations of antibodies. Their affinity constants could reach as high as 1012 M 1. The intermolecular forces involved in the binding of antigens to antibody include hydrophobic, Van der Waals, electrostatic and hydrogen binding (28-31). 

The interaction of homogeneous, murine myeloma immunoglobulins with such polysaccharide antigens as (2 6)- and (2 l)-j8-D-fructans, (1 6)-jS-o-... 

Antibodies and Immunoglobulins.— The interactions of homogeneous myeloma immunoglobulins with polysaccharide antigens have been reviewed. ... 

Immunoglobulins, homogeneous, murine myeloma, the interaction of, with polysaccharide antigens, 31, 313-346... 

On the anti-HSA-IgG-spacer-AL-2 latex, 16,000 antibodies were attached. The forward rate constant reduced for one antibody molecule (k =k /number of antibodies on the latex surface) was estimated to be 810 M s, which is much smaller than the observed reaction rate constant for the antigen-antibody reaction in the homogeneous system. Wolff et al. reported that 1.3 molecules of IgG per vesicle is enough for interaction of the vesicle with antigen-carrying cells (2i) ... 

Fig. 2.4. Competitive, homogeneous EIA. The symbol E represents enzyme, A antigen or hapten, S and CO substrate and enzyme cofactor, and Av and B avidin and biotin. Enzymes indicated with have modulated (increased or decreased) activities. In (a) hapten is conjugated to the enzyme and reaction with the antibody (shaded structure) modulates the enzyme activity. This interaction is, however, prevented if antigen is present in the sample. Similar principles apply if substrate (b) or cofactor (c) are conjugated with the antigen. In (d) antibody is directly linked to the enzyme, and the reaction of this antibody, particularly with high-molecular weight antigens, will block the active site of the enzyme. In (e) antibody, directed to haptens labeled to avidin, prevents avidin from inhibiting the biotin-containing enzyme, unless antibody is neutralized by the same hapten present in the sample.

Homogeneous, AM assays pose different requirements. Here, the enzyme should be easily conjugated near the active site without altering its activity. The reaction of hapten- or antigen-labeled enzyme with antibody should affect strongly the enzyme activity, e.g., through steric inhibition of the substrate at the catalytic site. The requirements for optimal ionic conditions and temperature for both enzyme activity and antigen-antibody interaction should be compatible. 

Enzyme activity is established under optimum conditions, as discussed for the various enzymes in Chapter 10, unless contraindicated in Section 14.3. However, these conditions should not be to the detriment of the antigen-antibody interaction, i.e., the pH should be close to neutrality and the ionic strength suitable. Homogeneous systems with assay conditions different from those described in Chapter 10 are given in Section 14.3. 

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