Abstract
Secretin immunoreactivity was detected in the central nervous system of the rat and pig with a highly specific radioimmunoassay. The secretin immunoreactivity in the rat and pig brain and duodenum extracts was fractionated by using a reverse-phase high-pressure liquid chromatographic system. The immunoreactive secretin from pig brain and duodenum coeluted precisely with synthetic porcine secretin. However, immunoreactive secretin extracted from rat brain and duodenum eluted slightly before porcine secretin. These data suggest a slight difference in the structure of rat and pig secretin. The detection of secretin in the brain lays the groundwork for studies to determine the role of the peptide in central nervous system function.
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