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Article

Mutant human protein disulfide isomerase assists protein folding in a chaperone-like fashion.

Journal of biotechnology - 25 Apr 1997

Gao Y, Quan H, Jiang M, Dai Y, Wang C C

Abstract excerpt

Human protein disulfide isomerase with an extra 10 amino acid residues of AEITRIDPAM at the N-terminal was expressed in E. coli as a soluble protein comprising 20% of total cell proteins, and was purified to near homogeneity through one step of DEAE-Sephacel chromatography. The mutant enzyme, which had the same CD spectrum and comparable disulfide isomerase and thiol-protein oxidoreductase activities with that of...

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Identifiers

PMID: 9195754
DOI: 10.1016/s0168-1656(97)01695-7

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutant human protein disulfide isomerase assists protein folding in a chaperone-like fashion.PMID 9195754Read ↗

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