Interactions between protein disulphide isomerase and peptides.
Eur J Biochem
; 248(1): 37-42, 1997 Aug 15.
Article
in En
| MEDLINE
| ID: mdl-9310357
ABSTRACT
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 with or 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.
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Collection:
01-internacional
Database:
MEDLINE
Main subject:
Peptides
/
Isomerases
Type of study:
Prognostic_studies
Limits:
Animals
Language:
En
Journal:
Eur J Biochem
Year:
1997
Document type:
Article
Affiliation country:
United kingdom