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However, no low molecular weight fragments with preserved immunoreactivity were found.Ĭopyright: All rights reserved. Digestion of CA 125 with proteolytic enzymes showed it to be particularly sensitive to trypsin cleavage. Antibodies belonging to the subgroup A4 were the only OC 125-like antibodies which reacted well with CA 125 in Western analysis. Strongest binding was observed with the M11-like antibodies, particularly M 11, K 96, K 97, MA602-6, 145-9. There was a marked difference between the antibodies in their ability to bind to CA 125 immobilized on a membrane. Western blot analysis showed staining both in the stacking gel and corresponding to a molecule of 200 kDa. Antibody affinity was estimated with labelled antigen in solution or with antigen adsorbed on microtiter wells. OV 198 and K 100 are most likely OC125-like and MA602-1 is Ml 1-like. Three antibodies were not studied by complete cross-inhibition due to low affinity (OV 198 and K 100) or lack of material (MA602-1). Antibody pairs from any two of the three groups may be used in immunometric assays. Antibody OV 197 binds to a domain designated C and is unique, as stated above. Only one antibody, ZR 38, would form an immunoassay combination with other M11 -like antibodies and thus represents a distinct subgroup. The M11 -like group of antibodies is more homogenous with strong cross-inhibition between most antibodies. Antibody B43.13 could form immunometric assay combinations particularly with antibodies of subgroup A4, indicating that the B43.13 epitope is in the periphery of the binding area of OC125-like antibodies. This conformational change was not observed with any other antibody combinations. Binding of nonlabelled OC 125 or K 95 to CA 125 caused a marked increase in binding of labelled OV 197 to the complex. The OC125-like group of antibodies has four subgroups with different binding specificities. One antibody, OV 197, showed binding specificity related to some of the OC125-like antibododies, but was classified into a separate group C. We conclude that the CA 125 antigen carries only two major anti-genic domains, which classifies the antibodies as OC125-like (group A) or Mil-like (group B). Immunometric assays using all possible antibody combinations were used to study the topography of antibody binding sites on the antigen. The binding specificity was studied using CA 125 immunoextracted by specific antibodies immobilized on various solid phases, or on the surface of human cell lines. The specificity of 26 monoclonal antibodies against the CA 125 antigen was investigated in two phases of the ISOBM TD-1 workshop.

Mtmr 13 antibody