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Updated: Aug 11, 2026

Purification of Native Complexes for Structural Study Using a Tandem Affinity Tag Method
Published on: July 27, 2016
Cation-dependent interactions of calreticulin with denatured and native proteins
Abstract:
Calreticulin has sequence homology with the molecular chaperone calnexin, which is known to control folding and assembly of nascent proteins in the endoplasmic reticulum in a calcium-dependent manner. We have investigated the interaction between human placental calreticulin and denatured placental and serum proteins under various incubation conditions. The interactions with denatured proteins differed significantly from the interactions with native proteins. The interactions were highly dependent on divalent metal ions or polyamines, but were not influenced by detergent and sulfhydryl agents. Our results indicate that calreticulin might have a similar role in protein folding as the chaperone calnexin.
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