| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 9121729 | FEMS Microbiology Letters | 2005 | 6 Pages |
Abstract
Functional properties of protein disulfide isomerase A (PDIA) from Aspergillus niger were investigated using ribonuclease A, glyceraldehyde 3-phosphate dehydrogenase (GAPDH) and prochymosin as substrates. PDIA was shown to function as an isomerase catalyzing the refolding of denatured and reduced ribonuclease A. PDIA also exhibited trx-independent chaperone activity preventing the aggregation of reduced, denatured GAPDH, an enzyme lacking disulfide bonds. Both isomerase activity and chaperone function of PDIA were essential for the efficient refolding of the reduced, denatured prochymosin.
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Authors
Yurong Liang, Wei Li, Qing Ma, Yuying Zhang,