This study reports the biosynthesis of two forms of pro-opiomelanocortin in the pars intermedia of the pituitary gland of the African clawed toad Xenopus laevis. The two forms could be resolved by dodecyl sulphate gel electrophoresis on a 9-16% acrylamide gradient and their molecular weights were 38200 and 37300. Incubation of neurointermediate lobes with [3H]glucosamine followed by tryptic digestion of the newly synthesized glycoproteins, revealed that both prohormones have only one glycosylated site, namely within the region corresponding to gamma 3-melanotropin. Biosynthesis of proteins in lobes treated with tunicamycin to prevent glycosylation again resulted in the production of two pro-opiomelanocortins (Mr 35000 and 34200), indicating that the two forms differ in their primary structure. This notion was corroborated by the results of tryptic mapping of the newly synthesized prohormones. The maps showed that the primary structures of the two forms of pro-opiomelanocortin differ in at least two parts of the molecules, one part concerning the endorphin region.
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