Insulin synthesis by recombination of A and B chains: a highly efficient method.
Open Access
- 1 June 1966
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 55 (6) , 1554-1561
- https://doi.org/10.1073/pnas.55.6.1554
Abstract
A procedure is described by which natural chains prepared by oxidative sulfitolysis of bovine insulin are recombined to produce insulin in yields ranging from 60 to 80% of theory. This procedure was applied with favorable results to the combination of the synthetic chains of sheep insulin with the corresponding chains of bovine insulin. The high recombination of yields strongly suggest that as far as insulin is concerned, the essential information for the proper alignment of the insulin chains to produce the protein is contained within the primary structure of the chains.This publication has 8 references indexed in Scilit:
- Resynthese von Insulin aus präoxydierter A‐Kette und reduzierter B‐KetteEuropean Journal of Organic Chemistry, 1966
- Insulin Peptides. XII. Human Insulin Generation by Combination of Synthetic A and B Chains1Journal of the American Chemical Society, 1966
- Insulin Peptides. XI. The Synthesis of the B Chain of Human Insulin and Its Combination with the Natural A Chain of Bovine Insulin to Generate Insulin Activity1Journal of the American Chemical Society, 1966
- BIOSYNTHESIS OF THE TWO CHAINS OF INSULINProceedings of the National Academy of Sciences, 1965
- On the problem of the chemical synthesis of proteins with special reference to insulinMetabolism, 1964
- Isolation of insulin from pancreatic extracts using carboxymethyl and diethylaminoethyl cellulosesBiochimica et Biophysica Acta (BBA) - General Subjects, 1964
- Resynthesis of insulin from its glycyl and phenylalanyl chains.1961
- Regeneration of Insulin Activity from the Separated and Inactive A and B ChainsNature, 1960