Tracking the disulfide rearrangement of heated lactoglobulin by matrix ‐assisted laser desorption/ionization‐in‐source decay top‐down analysis

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.
Source: Journal of Mass Spectrometry - Category: Chemistry Authors: Tags: APPLICATION NOTE Source Type: research
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