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Filtering by: Committee Member Buhler, Donald Academic Affiliation Environmental and Molecular Toxicology

A proteomic approach to 1,2-dichloroethane bioactivation and reaction with redox-active protein disulfide isomerase

Creator:

Kaetzel, Rhonda Sue

Abstract:

Protein disulfide isomerase (PDI), a member of the thioredoxin superfamily, contains two domains with significant sequence homology to the active sites in thioredoxin. PDI facilitates the folding of nascent proteins in the endoplasmic reticulum (ER), binds hormones and Ca²⁺, catalyzes the glutathione dependent reduction of dehydroascorbate, serves as a major...

Resource Type:

Dissertation

Full Text:

. Abstract approved: Donald J. Reed Protein disulfide isomerase (PDI), a member of the thioredoxin