Antigenic determinant sites

Definition of the association (or avidity) constant for such multivalent antibody—antigen reactions must consider not only the heterogeneity of the antibodies and the antigen determinant site(s), but also an apparent additive effect of binding two antigen molecules to a single antibody. Such effects lead... 

DEC is known to produce morphological changes on the surface of microfilariae. However, this change is not enough to cause death of the parasite [112]. It has also been shown that DEC enhances the specific IgG-mediated cell adherance on B.malayi microfilariae, which may be achieved by exposing the "hidden" antigenic determinant sites [119]. Martinez-Paloma [120] have shown that the immunogenic determinants of microfilariae of Onchocerca sp. are covered by an acellular cuticle. 

Competitive immunoassays may also be used to determine small chemical substances [10, 11]. An electrochemical immunosensor based on a competitive immunoassay for the small molecule estradiol has recently been reported [11]. A schematic diagram of this immunoassay is depicted in Fig. 5.3. In this system, anti-mouse IgG was physisorbed onto the surface of an SPCE. This was used to bind monoclonal mouse anti-estradiol antibody. The antibody coated SPCE was then exposed to a standard solution of estradiol (E2), followed by a solution of AP-labeled estradiol (AP-E2). The E2 and AP-E2 competed for a limited number of antigen binding sites of the immobilized anti-estradiol antibody. Quantitative analysis was based on differential pulse voltammetry of 1-naphthol, which is produced from the enzymatic hydrolysis of the enzyme substrate 1-naphthyl phosphate by AP-E2. The analytical range of this sensor was between 25 and 500pg ml. 1 of E2. 

The nature of the antigenic determinant has been characterized in a male worker with occupational asthma from nickel [415, 416] the antibody recognized Ni2+ bound at the natural Cu2 + /Ni2+ transport site of human albumin. The interpretation was deduced from metal ion blocking experiments and from the good agreement obtained between the pH dependency of the formation of the Ni2 + -albumin complex and the antigen-antibody complex. It was suggested that the antibody interaction depended on a special structural feature of the interaction of Ni2 + with human serum albumin, and perhaps the ability to form an octahedral complex affords one explanation [417]. 

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