Interactions between protein disulphide isomerase and peptides

Klappa, Peter and Hawkins, Hilary C. and Freedman, Robert B. (1997) Interactions between protein disulphide isomerase and peptides. European Journal of Biochemistry, 248 (1). pp. 37-42. ISSN 0014-2956. (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)

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There is growing evidence that protein disulphide isomerase (PDI) has a common chaperone function in the endoplasmic reticulum. To characterise this function, we investigated the interaction of purified PDI with radiolabelled model peptides, somatostatin and mastoparan, by cross-linking. The interaction between the peptides and PDI was specific, for it showed saturation and was abolished by denaturation of PDI. The interaction between a hydrophobic peptide without cysteine residues was much more sensitive to Triton X-100 than the interaction between PDI and a more hydrophilic peptide wither without cysteine residues. We therefore propose that hydrophobic interactions between protein disulphide isomerase and peptides play an important role in the binding process. The interaction between PDI and the bound peptide therefore is enhanced by the formation of mixed disulphide bonds.

Item Type: Article
Uncontrolled keywords: protein disulphide isomerase; somatostatin; peptide binding; cross-linking
Subjects: Q Science
Q Science > QH Natural history > QH301 Biology
Divisions: Faculties > Science Technology and Medical Studies > School of Biosciences
Depositing User: M.A. Ziai
Date Deposited: 21 Apr 2009 02:18
Last Modified: 28 May 2014 09:40
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