Zapun, Andre, Creighton, Thomas E., Rowling, Pamela J. E., Freedman, Robert B. (1992) Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum. Proteins: Structure, Function, and Bioinformatics, 14 (1). pp. 10-15. ISSN 0887-3585. (doi:10.1002/prot.340140104) (The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided) (KAR id:22291)
| The full text of this publication is not currently available from this repository. You may be able to access a copy if URLs are provided. | |
| Official URL: http://dx.doi.org/10.1002/prot.340140104 |
Abstract
The rates of folding and disulfide bond formation in reduced BPTI were measured in vitro in the presence and absence of total protein from the endoplasmic reticulum. The rates were increased substantially by the endoplasmic reticulum proteins, but only to the extent expected from the known content and activity of protein-disulfide-isomerase. No effects of added ATP or Ca2+ were observed, even though protein-disulfide-isomerase binds Ca2+ tightly.
| Item Type: | Article |
|---|---|
| DOI/Identification number: | 10.1002/prot.340140104 |
| Uncontrolled keywords: | protein disulfide isomerase; disulfide bonds; protein folding; chaperones |
| Subjects: | Q Science > QH Natural history > QH301 Biology |
| Divisions: | Divisions > Division of Natural Sciences > Biosciences |
| Depositing User: | O.O. Odanye |
| Date Deposited: | 27 Jul 2009 17:12 UTC |
| Last Modified: | 05 Nov 2024 10:01 UTC |
| Resource URI: | https://kar.kent.ac.uk/id/eprint/22291 (The current URI for this page, for reference purposes) |
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