Use of anti-idiotypic antibodies to establish that monoclonal antibody 7H11D6 binds to the. cap alpha. /sub 2/-macroglobulin receptor recognition site
Studies were performed to determine if monoclonal antibody 7H11D6 binds to the region of ..cap alpha../sub 2/-macroglobulin (..cap alpha../sub 2/M) that interacts with cell-surface receptors. Chemical modification studies revealed that the epitope region for 7H11D6 is sensitive to modification of the inhibitor with cis-dichlorodiammineplatinum (II). To determine if the epitope for 7H11D6 is comprised of residues involved in the ..cap alpha../sub 2/M receptor determinant, anti-idiotypic antibodies against 7H11D6 were prepared. A competitive enzyme-linked immunosorbent assay demonstrated that the anti-idiotypic IgG competed with ..cap alpha../sub 2/M-trypsin complexes for binding to 7H11D6. The anti-idiotypic IgG inhibited the binding of /sup 125/I-labeled ..cap alpha../sub 2/M-trypsin complexes to normal rat kidney fibroblasts, and a K/sub d/ of 194 pM for the binding of the anti-idiotype to these cells was derived from a fit of the data to a model involving a single class of sites. Binding of the anti-idiotypic IgG to the ..cap alpha../sub 2/M receptor provides unequivocal evidence that 7H11D6 is binding to residues within the receptor recognition site on ..cap alpha../sub 2/M and not merely to residues sufficiently close to that region to cause steric hindrance.
- Research Organization:
- American Red Cross Biomedical Research and Development, Rockville, MD (USA)
- OSTI ID:
- 6922276
- Journal Information:
- J. Biol. Chem.; (United States), Vol. 263:14
- Country of Publication:
- United States
- Language:
- English
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