The Biosynthesis of C14- and H3-Labeled Insulin
In recent years, there has been much interest in the biosynthesis of insulin because of its role in diabetes. In addition, the exact amino acid sequence of the two peptide chains is known  and, therefore, the insulin molecule has become a model protein for research in synthetic mechanisms. Many techniques for the purification and characterization of insulin have been developed [2,3,4]. In the study of insulin biosynthesis, several investigators have incubated mammalian pancreas slices in the presence of radioactive amino acids in vitro, and then isolated the labeled insulin [3,5,6] This approach is limited because the beta cells of the islets of Langerhans (which manufacture and store insulin) comprise only a small fraction of the total pancreas. During the development of the pancreas in certain teleost fish, however, the islet tissue becomes separated from the exocrine pancreas and it appears in the adult as a macroscopic aggregate of endocrine tissue called the principal islet or Brockmann body. The principal islet contains cells which are functionally and anatomically analogous to the B-cells of mammalian islets; fish insulin is similar to mammalian insulin in structure and in biological activity [7,8]. Our studies on insulin biosynthesis using fish islets were begun in 1959; this report is a summary of these investigations.
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