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- W754035451 abstract "Proinsulin and insulin-precursors with deletions in the C-peptide region were expressed and secreted from yeast. The structure of the secreted insulin-like peptides was determined by sequence analysis to evaluate the disulphide bond formation and the pattern of posttranslational processing. Processing at the Arg-Arg and Lys-Arg sequences of proinsulin was found to occur before disulphide bond formation thus resulting in a high amount of C-peptide and a low amount of disulphide bridge-linked B- and A-chains. In contrast insulin-precursors in which the C-peptide region had been deleted (e.g. B-chain-Lys-Arg-A-chain) were secreted in high amounts as single chain molecules with the same location of disulphide bonds as insulin. It is concluded that the C-peptide region of proinsulin is not necessary for folding and disulphide bond formation. The results further indicate that the Lys-Arg sequence — when located in the disulphide bridge-linked B-Lys-Arg-A precursor molecule — is inaccessible for posttranslational processing by the yeast enzyme systems." @default.
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- W754035451 date "1987-01-01" @default.
- W754035451 modified "2023-09-27" @default.
- W754035451 title "The Use of Site-Directed Mutagenesis to Study Disulphide Bond Formation and Posttranslational Processing of Insulin Precursors Expressed and Secreted from Yeast" @default.
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- W754035451 doi "https://doi.org/10.1007/978-1-59259-480-1_43" @default.
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