| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 1178766 | Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics | 2011 | 9 Pages |
Abstract
⺠Both PDI and PDIp can inactivate thermally-unfolded RNase that preserves native disulfide bonds. ⺠The N-terminal active site of PDIp plays a principal role in inactivating RNase. ⺠Stable disulfide-linked complexes are formed between PDI/PDIp and RNase. ⺠RNase can be released and reactivated from the PDI/PDIp-RNase complexes.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Xin-Miao Fu, Bao Ting Zhu,