States of tryptophyl residues and stability of recombinant human matrix metalloproteinase 7 (Matrilysin) as examined by fluorescence

Journal of Biochemistry

Volumn 128, Issue 3, 2000, Pages 363-369

  Inouye, K ^a   Tanaka, H ^a   Oneda, H ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Denaturation; Fluorescence quenching; Matrilysin; Matrix metalloproteinase; Protein stability

Indexed keywords

MATRILYSIN; RECOMBINANT MATRILYSIN; TRYPTOPHAN; UNCLASSIFIED DRUG;

AMINO ACID COMPOSITION; ARTICLE; ENZYME ANALYSIS; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; STRUCTURE ANALYSIS;

EID: 0033819120     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022762     Document Type: Article

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