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Folding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum

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: 16 Nov 2021 10:00 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/22291 (The current URI for this page, for reference purposes)

University of Kent Author Information

Freedman, Robert B..

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