Abstract
The expression of antigenic determinants on size variants of human growth hormone (hGH) has been investigated using monoclonal antibodies of distinct combining-site specificity. Monomeric, dimeric, trimeric and polymeric (very high-molecular-weight) forms of hGH were separated by gel filtration on Sephadex G-100, and their antigenic potency was determined quantitatively by competition with 125I-labelled hGH for binding to each of four different monoclonal antibodies. With three of these antibodies the potencies of monomeric, dimeric and trimeric hGH were not significantly different, and the polymeric material was 11–13% as potent as the monomer. However, using one antibody (NA 71) the antigenic potencies of dimeric and trimeric hGH were lower (30–50%) than that of the monomer, and the polymeric material was only about 5% as potent as the monomer. These results suggest that the determinant with which antibody NA 71 interacts is close to the site of interaction between hGH monomers and apparently partially ‘masked’ in dimers, trimers and polymeric hGH.
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