Both chaperone and isomerase functions of protein disulfide isomerase are essential for acceleration of the oxidative refolding and reactivation of dimeric alkaline protease inhibitor

Protein Science

Volumn 13, Issue 9, 2004, Pages 2493-2501

  Pandhare, Jui ^a,b   Deshpande, Vasanti ^a  

^a NATIONAL CHEMICAL LABORATORY   (India)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

Aggregation; Chemoaffinity labeling; Foldase; Protein folding catalyst

Indexed keywords

5 IODOACETAMIDOFLUORESCEIN; ALKALINE PROTEINASE INHIBITOR; BACTERIAL ENZYME; BUFFER; CHAPERONE; FLUORESCEIN DERIVATIVE; PROTEIN DISULFIDE ISOMERASE; PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

ARTICLE; DIMERIZATION; DISULFIDE BOND; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME REACTIVATION; ENZYME RECONSTITUTION; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN REFOLDING; REACTION ANALYSIS; STOICHIOMETRIC EXCESS; STOICHIOMETRY; STREPTOMYCES;

BACTERIAL PROTEINS; BUFFERS; DIMERIZATION; DISULFIDES; ENZYME ACTIVATION; FLUORESCEINS; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PROTEIN DENATURATION; PROTEIN DISULFIDE-ISOMERASE; PROTEIN FOLDING;

BACTERIA (MICROORGANISMS); STREPTOMYCES;

EID: 4344616323     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.03552004     Document Type: Article

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