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Overexpression of Protein Disulfide Isomerase in Aspergillus
Current Microbiology, 2000One of the major problems with the production of biotechnologically valuable proteins has been the purification of the product. For Escherichia coli and Saccharomyces cerevisiae, there are several techniques for the purification of intracellular proteins, but these are time consuming and often result in poor yields.
Hala El-Adawi +2 more
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[4] Thermophilic fungal protein disulfide isomerase
1998Publisher Summary For the study the authors have isolated and characterized a thermostable protein disulfide isomerase (PDI) from a thermophilic fungus, Humicola insolens. The cDNA encoding the fungal PDI has been cloned and expressed in Bacillus brevis. PDIs from vertebrates and yeast are relatively heat labile.
Masana Hirai +5 more
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Protein disulfide isomerase is both an enzyme and a chaperone
The FASEB Journal, 1993Protein disulfide isomerase (PDI) catalyzes the formation of native disulfides of peptide chains from either the reduced form or randomly joined disulfides. So that thiols situated at distant parts of the polypeptide chain can be joined together to form the native disulfides, the polypeptide chain has to be folded, at least to some extent, into the ...
Chih-Chen Wang, Chen-Lu Tsou
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[3] Protein disulfide isomerase
1998Protein disulfide isomerase (PDI) is a multifunctional protein that facilitates the formation of correct disulfide crosslinks between cysteine residues during the early stages of protein folding and secretion in the endoplasmic reticulum. It is a member of a large family of oxidoreductases that catalyse exchange reactions between thiols and disulfides.
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Protein disulfide isomerase: the structure of oxidative folding
Trends in Biochemical Sciences, 2006Cellular functions hinge on the ability of proteins to adopt their correct folds, and misfolded proteins can lead to disease. Here, we focus on the proteins that catalyze disulfide bond formation, a step in the oxidative folding pathway that takes place in specialized cellular compartments.
Gruber, Christian W +4 more
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Promotion of insulin aggregation by protein disulfide isomerase
Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 2007We examined the aggregation of insulin as a result of reduction of disulfide bonds catalyzed by protein disulfide isomerase (PDI) using various techniques. We demonstrated the kinetic correlation between PDI-catalyzed insulin reduction and the aggregate formation, the relationship between aggregation and amyloid formation, and the structural ...
Kazuyoshi Ado +3 more
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Bacitracin is not a specific inhibitor of protein disulfide isomerase
The FEBS Journal, 2010To successfully dissect molecular pathways in vivo, there is often a need to use specific inhibitors. Bacitracin is very widely used as an inhibitor of protein disulfide isomerase (PDI) in vivo. However, the specificity of action of an inhibitor for a protein‐folding catalyst cannot be determined in vivo.
Lloyd W. Ruddock, Anna-Riikka Karala
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The Role of Protein Disulfide Isomerase in Yeast
1993Most disulfide-containing proteins are extracellular and most extracellular proteins contain disulfide bonds. Secretory enzymes, polypeptide hormones, immunoglobulines, and other serum proteins all have disulfide bonds. These extracellular and cell surface proteins are translated on membrane-bound ribosomes and concurrently translocated into the lumen ...
H. Tachikawa, Tadashi Miura, T. Mizunaga
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Purification and Characterization of Yeast Protein Disulfide Isomerase
The Journal of Biochemistry, 1990Protein disulfide-isomerase (PDI), which reactivates inactive scrambled RNase, was purified from Saccharomyces cerevisiae. The enzyme was purified 1,850-fold to apparent homogeneity by five purification steps: 30-70% ammonium sulfate fractionation, DEAE Toyopearl-650S and Butyl Toyopearl-650S chromatographies, and differential Phenyl-5PW HPLC with or ...
Takemitsu Mizunaga +3 more
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Protein disulfide isomerase: A multifunctional protein of the endoplasmic reticulum
1996Protein disulfide isomerase (PDI) is a resident enzyme of the endoplasmic reticulum (ER) that was discovered over three decades ago. Contemporary biochemical and molecular biology techniques have revealed that it is present in all eukaryotic cells studied and retained in the ER via a -KDEL or -HDEL sequence at its C-terminus.
J. M. Luz, W. J. Lennarz
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