pH-induced conformational transitions of the propeptide of human cathepsin L. A role for a molten globule state in zymogen activation

Journal of Biological Chemistry

Volumn 273, Issue 19, 1998, Pages 11498-11504

  Jerala, Roman ^a   Žerovnik, Eva ^b   Kidrič, Jurka ^a   Turk, Vito ^b  

^a NATIONAL INSTITUTE OF CHEMISTRY   (Slovenia)

^b JO EF STEFAN INSTITUTE   (Slovenia)

Author keywords

[No Author keywords available]

Indexed keywords

CATHEPSIN L; ENZYME PRECURSOR;

ARTICLE; CIRCULAR DICHROISM; ENZYME ACTIVITY; ENZYME REGULATION; ENZYME STRUCTURE; ENZYME SYNTHESIS; FLUORESCENCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PH; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING;

CATHEPSINS; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; DEXTRAN SULFATE; ENDOPEPTIDASES; ENZYME ACTIVATION; HUMANS; HYDROGEN-ION CONCENTRATION; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN PRECURSORS; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE;

EID: 0032496158     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.19.11498     Document Type: Article

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