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Redox regulation plays an important role across a broad spectrum of biology. Accumulating evidence suggests that thioredoxin, a widely distributed redox enzyme, participates in the redox control of numerous target proteins, thus, playing a key role as a signaling intermediate that senses the metabolic state or environmental changes, and transmits information to induce appropriate reactions for survival. The recent development of proteomic strategies has facilitated the identification of thioredoxin targets to allow clarification of new thioredoxin-dependent redox mechanisms. This review examines the usefulness of a disulfide proteome technique for the analysis of thioredoxin-dependent redox regulation as well as for use in allergen studies.
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Yano et al. (2008) studied this question.
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