Skip to main content

Influence of protein disulfide isomerase (PDI) on antibody folding in vitro

Lilie, Hauke, McLaughlin, Stephen H., Freedman, Robert B., Buchner, Johannes (1994) Influence of protein disulfide isomerase (PDI) on antibody folding in vitro. Journal of Biological Chemistry, 269 (19). pp. 14290-14296. ISSN 0021-9258. (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:19855)

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.

Abstract

The role of eucaryotic protein disulfide isomerase (PDI) in the folding and reoxidation of proteins in vitro was investigated using an antibody Fab fragment as a model substrate, since PDI is known to participate in the disulfide bond formation of immunoglobulins in vivo. PDI has no effect on the folding of the Fab fragment with intact disulfide bonds, suggesting that, at least in this system, PDI is not able to influence the folding process in a chaperone-like manner. Instead, the role of PDI is limited to disulfide bond formation as demonstrated for the folding of the denatured and reduced Fab fragment. Here, PDI influences the yield of reactivation enormously with a maximum effect at about stoichiometric amounts of PDI and Fab. Furthermore, PDI changes the redox dependence of the reaction. In the presence of PDI, formation of the correct disulfide bonds is possible at higher oxidizing conditions compared to the spontaneous reaction. The requirements both for stoichiometric amounts of PDI and for the presence of PDI during the first seconds of refolding suggest that there is a kinetic competition between rapid structure formation of the antibody domains and interaction of PDI with cysteine residues in the folding protein.

Item Type: Article
Subjects: Q Science > QP Physiology (Living systems) > QP517 Biochemistry
Q Science > QP Physiology (Living systems) > QP506 Molecular biology
Divisions: Divisions > Division of Natural Sciences > Biosciences
Depositing User: O.O. Odanye
Date Deposited: 08 Jul 2009 13:17 UTC
Last Modified: 16 Nov 2021 09:58 UTC
Resource URI: https://kar.kent.ac.uk/id/eprint/19855 (The current URI for this page, for reference purposes)

University of Kent Author Information

Freedman, Robert B..

Creator's ORCID:
CReDIT Contributor Roles:
  • Depositors only (login required):

Total unique views for this document in KAR since July 2020. For more details click on the image.