The biosynthesis of glucagon was examined using pigeon isolated islet preparation. Studies showed that radioactive tryptophan was incorporated into a large gel-filtration component, possessing glucagon immunoactivity. The radioactive component appeared homogeneous on Sephadex G-100 gelfiltration and polyacrylamide gel electrophoreses, and has a molecular weight of approximately 69,000. Tryptic hydrolysates of the large biosynthetic component contained radioactive peptides identifiable chromatographically with those obtained from a tryptic hydrolysate of bovine-porcine glucagon. These data suggested the biosynthesis of a high molecular weight glucagon-related protein in avian islets of Langerhans.
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Avery Tung (1973) studied this question.