Antigen binding capacity

Jagannath, C., and Sehgal, S. (1989) Enhancement of the antigen-binding capacity of incomplete IgG antibodies to Brucella melitensis through Fc region interactions with Staphylococcal protein A. J. Immunol. Meth. 124, 251-257. 

In order to compare the specific activity of plant-derived C5-1 to that of the hybridoma-derived antibody, the antigen-binding capacity of antibodies produced in each system was assayed by enzyme-linked immunosorbent assay (ELISA). As shown in Table 1.2, antibodies from both sources demonstrated similar binding characteristics against human IgGs [8]. Furthermore, the stability of alfalfa-derived C5-1 in the blood stream of Balb/c mice was comparable to that of the hybridoma-derived IgG [8]. 

As mentioned previously, the main disadvantage of these immobilization methods is the non-specific nature of the binding reaction, which often results in multiple site attachments and multiple orientations. As a consequence, the immobilized antibodies show a decrease or complete loss of their antigen-binding capacity. To eliminate these drawbacks, several approaches leading to oriented antibody coupling have been developed over the last few years [99]. 

Protein A binds to the F,. region of IgG and does not interfere with the antigen binding capacity of IgG, thus FITC-Protein A can form tertiary complexes with antigen and antibody (IgG) . FITC-labeled protein A has been applied in different immunochemical studies and separations of cells bearing IgG or other... 

---