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. 1969 Jun;63(2):442–449. doi: 10.1073/pnas.63.2.442

BIOSYNTHESIS OF INSULIN IN BOVINE FETAL PANCREATIC SLICES: THE INCORPORATION OF TRITIATED LEUCINE INTO A SINGLE-CHAIN PROINSULIN, A DOUBLE-CHAIN INTERMEDIATE, AND INSULIN IN SUBCELLULAR FRACTIONS*

A K Tung 1,2, C C Yip 1,2
PMCID: PMC223584  PMID: 5257135

Abstract

This communication reports the biosynthesis of insulin in the bovine fetal pancreatic slices in vitro. Double-chain proinsulin and insulin were found as major components in the mitochondrial-granule fraction of bovine fetal pancreas. Tritiated leucine was incorporated into a single-chain proinsulin, a double-chain proinsulin, and insulin. Subcellular fractionation of the slices incubated with tritiated leucine showed that radioactive single-chain proinsulin was present in the deoxycholate-soluble microsomal fraction, deoxycholate-insoluble microsomal fraction, and mitochondrial-granule fraction. Labeled double-chain proinsulin and insulin were present in the deoxycholate-soluble microsomal and mitochondrial-granule fractions. These results are consistent with the hypothesis that insulin is synthesized as a single-chain polypeptide on the ribosomes, and that intracellular proteolysis in the subcellular membranous organelles and beta-granules converts the single-chain proinsulin to insulin via a double-chain intermediate.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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