Protein Disulfide Isomerase from bovine liver has been used:
- to study the functional role of PDI in parasite infection and the interaction between macrophage PDI andL. chagasi
- in the in vitro translation reaction for the generation of disulfide bonds
- in insulin-disulfide reduction assay and peptide binding assay
- as a positive control in thiol-disulfide oxidoreductase activity assay
Protein disulfide isomerase (PDI) from bovine liver is a homodimer with a molecular weight of 107 kDa with the monomer corresponding to 57 kDa. The isoelectric point (pI) is approximately 4.2. The enzyme is a glycoprotein with 12% total carbohydrate content comprising of mannose, galactose, N-acetyl neuraminic acid (NANA) and 2-acetamido-2-deoxyglucose. PDI is an ubiquitous redox chaperone enzyme. It belongs to the, thioredoxin superfamily and is high conserved.
Protein Disulfide Isomerase (PDI) is mainly located in the endoplasmic reticulum (ER), where it assists in protein-folding and thiol-disulfide exchanges. It aids protein refolding in vitro allowing recombinant proteins to achieve their native state.
Disulfide Oxidoreductase produced in E.Coli is a periplasmic protein isolated from E. coli, containing 208 amino acids having a molecular mass of 23,149 Dalton.
The DsbA is purified by proprietary chromatographic techniques.
DsbA appears to be necessary for correct formulation of disulfide bonds in exported proteins in vivo. DsbA is useful as a standard in immunoblotting. This protein catalyses the reduction and exchange of disulfide bonds and the oxidation of free sulfhydryl groups in vitro. It is the strongest oxidant of the thioredoxin superfamily. This thio/disulfide oxidoreductase is required for efficient disulfide bond formation in the periplasm of E. coli.
