Abstract
A metalloantibody has been constructed with a coordination site for metals in the antigen binding pocket. The Zn(II) binding site from carbonic anhydrase B was used as a model. Three histidine residues have been placed in the light chain complementarity determining regions of a single chain antibody molecule. In contrast to the native protein, the mutant displayed metal-dependent fluorescence-quenching behavior. This response was interpreted as evidence for metal binding in the three-histidine site with relative affinities in the order Cu(II) > Zn(II) > Cd(II). The presence of metal cofactors in immunoglobulins should facilitate antibody catalysis of redox and hydfolytic reactions.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 659-666 |
| Number of pages | 8 |
| Journal | Science |
| Volume | 249 |
| Issue number | 4969 |
| State | Published - Aug 10 1990 |
All Science Journal Classification (ASJC) codes
- General