Abstract
The specificities of two antibodies directed to the gastrointestinal hormone, gastrin, were examined by evaluation of a series of human gastrin peptide fragments as inhibitors in a radioimmunoassay. Both antibodies showed similar inhibition with synthetic human gastrin and were directed to the C-terminal part of the molecule. The rabbit antibody recognized the C-terminal dipeptide and very little increase in inhibition was demonstrated with peptides larger than the tetrapeptide. The guinea pig antibody recognized no peptide smaller than the tetrapeptide at the highest concentration studied (4 × 10 3 pmole/ml). A graded increase in inhibitory activity was seen from the tetra to the octapeptide, which increased further with the whole heptadecapeptide. These differences in the size of the peptide required for binding may reflect differences in the size of the combining sites of the two antibodies.
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