The possibility of obtaining calcitonin and/or calcitonin-gene-related peptide (CGRP) immunorelated molecules from partly digested proteins was investigated with fish and shrimp hydrolysates. These two peptides were quantified by both radioimmunoassay and radioreceptor assay; the positive extracts were partly purified. Different hydrolysates were analysed: cod head, stomach and viscera hydrolysates, a shrimp hydrolysate and two sardine hydrolysates. Although each cod extract interacted in the CGRP radioimmunoassay, none of these extracts was able to displace the CT binding to its antibody. In contrast, shrimp and sardine hydrolysates interacted with both radioimmunoassays. Radioreceptor assays performed on the same extracts demonstrated that only three extracts contained the structural determinants that allowed them to interact in the CGRP radioreceptor assay. No interaction with the calcitonin radioreceptor assay could be demonstrated. Molecular sieving of the two sardine extracts showed that the immunoreactivity was resolved into two main fractions. The higher-molecular-mass fraction interacted only in the CGRP radioreceptor assay. The results obtained suggest the presence of a biologically related CGRP molecule in peptone hydrolysates and requires further investigation into the role of these peptide fragments in the regulation of intestinal function by partly digested proteins.
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