Affiliation:
1. School of Chemistry and Chemical Engineering Guangxi University Nanning China
2. Institute for Cell Analysis Shenzhen Bay Laboratory Shenzhen China
Abstract
AbstractDisulfide bond rearrangement is a common occurrence during protein analysis or treatment. A convenient and rapid method has been developed to investigate heat‐induced disulfide rearrangement of lactoglobulin using matrix‐assisted laser desorption/ionization‐in‐source decay (MALDI‐ISD) technology. By analyzing heated lactoglobulin in reflectron and linear mode, we demonstrated that cysteines C66 and C160 exist as free residues other than linked ones in some protein isomers. This method provides a straightforward and expeditious way to assess the cysteine status and structural changes of proteins under heat stress.