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Identification of intramolecular disulfide bonds in GrxS12

ABSTRACT: To investigate whether the conserved Cys residues of Grxs form intramolecular or intermolecular disulfide bonds, the recombinant GrxS12 proteins were purified, and subsequently separated using non-reducing SDS-PAGE. The gel revealed the presence of a monomer band but not a dimer band, indicating the absence of intermolecular disulfide bonds. The protein from the monomer band was subjected to proteolytic digestion and subsequent analysis by spectrometry. The spectrometric data revealed that the GrxS12 formed an intramolecular disulfide linkage between the T31WJC34SYSSQVK41 and H88IGGC92SDTLQLHNKGELEAILAEANGK114 peptides.

INSTRUMENT(S):

ORGANISM(S): Arabidopsis Thaliana (mouse-ear Cress)

TISSUE(S): Plant Cell

SUBMITTER: Yanshuang Liu

LAB HEAD: Shaojun Dai

PROVIDER: PXD058877 | Pride | 2026-01-16

REPOSITORIES: Pride

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			Action	DRS
	20240930-LYS-grxs12.msf	Msf
	20240930-LYS-grxs12.raw	Raw
	LYS-GRXS12_S-S_2024.10.01.csv	Csv

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