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Isolation and Characterization of Immunoreactive Somatostatin from

A B S T R A C T Using a radioimmunoassay with labeled synthetic tetradecapeptide somatostatin, a large amount of immuinoreactive somatostatin was found in the principal pancreatic islet of the channel catfish (Ictalurus punctata). The purpose ofthese experiments was to isolate and characterize the somatostatin-like material. Extracts of islets were chromatographed on a BioGel P-30 column, and over 90% ofthe immunoreactive somatostatin migrated with proteins at least twice the size of synthetic tetradecapeptide somatostatin. This fraction was further purified by ion-exchange chromatography on carboxymethyl-cellulose and DEAEcellulose columns. Two peptides were obtained with identical immunoreactivity, which was -25% that of the synthetic somatostatin. Each peptide wasjudged to be >95% pure by thin-layer electrophoresis, polyacrylamide gel electrophoresis at pH 8.9, and highpressture liquid chromatography. Further criteria of purity included amino-terminal analysis of fraction IV yielding only aspartic acid. A total of 1.3 mg of fraction II, and 3.8 mg of fraction IV somatostatin-like peptides were ob)tained from 10 g of fresh frozen islets. Characterization of the two peptides revealed both peptides slightly more acidic than synthetic tetradecapeptide somatostatin. Fraction II had an isoelectric point of 8.0-8.3, and fraction IV 8.3-9.0. Molecular weight estimation by sodium dodecyl sulfate-urea polyacrylamide gel electrophoresis revealed similar mobility ofboth peptides, between pancreatic polypeptide (mol