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Volumn 39, Issue 40, 2000, Pages 12382-12390

The residual pro-part of cathepsin C fulfills the criteria required for an intramolecular chaperone in folding and stabilizing the human proenzyme

(3) Cigic, B a,c Dahl, S W b Pain, R H a

a JO EF STEFAN INSTITUTE (Slovenia)

b Unizyme Laboratories A/S (Denmark)

c UNIVERSITY OF LJUBLJANA (Slovenia)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONE; DIPEPTIDYL PEPTIDASE I; ENZYME PRECURSOR;

ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; STRUCTURE ANALYSIS;

CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; COLORIMETRY; DIPEPTIDYL PEPTIDASE I; DITHIOTHREITOL; ENZYME PRECURSORS; ENZYME STABILITY; GUANIDINE; HUMANS; KINETICS; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN RENATURATION; RECOMBINANT PROTEINS; REDUCING AGENTS; THERMODYNAMICS; UREA;

EID: 0034633884 PISSN: 00062960 EISSN: None Source Type: Journal
DOI: 10.1021/bi0008837 Document Type: Article

Times cited : (32)

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