Fig. 5: Each disulfide bond in MTP folded by PDI is important for the structural stability of MTP. | Nature Communications

Fig. 5: Each disulfide bond in MTP folded by PDI is important for the structural stability of MTP.

From: Differential transport pathways of saturated and unsaturated fatty acid esters in male mouse hepatocytes

Fig. 5

a Positions of 10 cysteines in human MTP protein. b Seven peptides containing one or two cysteines of MTP and one peptide with no cysteine were synthesized and used for differential cysteine alkylation and PRM-MS analysis. c Schematic of the PRM-MS workflow. d Redox state of 9 cysteines in MTP were measured by PRM-MS (n = 3 biological replicates in each group). e The WT and mutant MTP plasmids were transfected into HepG2 cells, and the expressions of WT and mutant MTP proteins were detected by Western blotting with an anti-FLAG antibody. f The relative abundance of each MTP protein was quantitated by the intensity of each WB band. n = 3 biological replicates in each group. Two-tailed Student’s t test were used. Data are presented as mean ± SEM. Source data are provided as a Source Data file.

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