Abstract
Antibodies to human fetal aortic elastin were isolated from sheep immunized with alpha-elastin peptides. In preliminary tests of specificity using passive hemagglutination, partial cross-reactivity was demonstrated with alpha-elastin from other species. However, in a double antibody radio-immunoassay alpha-elastin peptides from other mammalian species failed to compete with 125I-labelled human alpha elastin. These results suggest the existence of at least two different antigenic sites on the elastin molecule. One, a high affinity site, demonstrates species specificity at low antigen/antibody concentrations. The other, a low affinity site, is common to mammalian elastins and is demonstrated at high antibody/antigen concentrations. In the radioimmunoassay the antibodies showed considerably less avidity for adult human alpha-elastin than for the fetal antigen. This implies that the species specific site is age-dependent and probably involves the cross-linking region of the elastin molecule. Using the sheep antiserum immunohistochemical staining of elastic tissue has been developed. This should prove to be a useful technique for studying polymeric elastin in intact tissue by light microscopy and at the ultrastructural level.
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