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• W2022109729 startingPage "3927" @default.
• W2022109729 abstract "Native insulin denatures and unfolds in the presence of thiol catalyst via disulfide scrambling (isomerization). It undergoes two transient non‐native conformational isomers, followed by an irreversible breakdown of the protein to form oxidized A‐ and B‐chain. Denaturation and breakdown of native insulin may occur under physiological conditions. At 37 °C, pH 7.4, and in the presence of cysteine (0.2 mM), native insulin decomposes with a pseudo first order kinetic of 0.075 h −1 . At 50 °C, the rate increases by 5‐fold. GdnCl and urea induced denaturation of insulin follows the same mechanism. These results demonstrate that stability and unfolding pathway of insulin in the presence of endogenous thiol differ fundamentally from its reversible denaturation observed in the absence of thiol, in which native disulfide bonds of insulin were kept intact during the process of denaturation." @default.
• W2022109729 created "2016-06-24" @default.
• W2022109729 creator A5024831791 @default.
• W2022109729 creator A5041380617 @default.
• W2022109729 date "2005-06-20" @default.
• W2022109729 modified "2023-09-26" @default.
• W2022109729 title "Unfolding and breakdown of insulin in the presence of endogenous thiols" @default.
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• W2022109729 doi "https://doi.org/10.1016/j.febslet.2005.06.010" @default.
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