Evidence that thermodynamic stability of papaya glutamine cyclase is only marginal

Biopolymers

Volumn 65, Issue 5, 2002, Pages 325-335

  Azarkan, Mohamed ^a   Amrani, Amina ^a   Zerhouni, Samira ^a   Oberg, Keith A ^a   Ruysschaert, Jean Marie ^a   Wintjens, René ^b   Looze, Yvan ^a  

^a FREE UNIVERSITY OF BRUSSELS   (Belgium)

^b INSTITUT DE BIOLOGIE DE LILLE   (France)

Author keywords

Carica papaya; Denaturation; Electrostatic interaction; Glutamine cyclase; Molten globule state; Protein folding

Indexed keywords

CATALYSIS; ENZYMES; FLUORESCENCE; SOLUTIONS; SPECTROSCOPY; THERMODYNAMIC STABILITY;

PROTEOLYSIS;

BIOPOLYMERS;

8 ANILINO 1 NAPHTHALENESULFONIC ACID; GLUTAMINE CYCLASE; GLYCOPROTEIN; GUANIDINE; UNCLASSIFIED DRUG;

AQUEOUS SOLUTION; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENZYME ANALYSIS; ENZYME BINDING; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; FLUORESCENCE SPECTROSCOPY; MEASUREMENT; MOLECULAR WEIGHT; NONHUMAN; PAPAYA; PROTEIN DEGRADATION; PROTEIN FOLDING; PROTEIN FUNCTION; THERMODYNAMICS;

AMINOACYLTRANSFERASES; CARICA; CIRCULAR DICHROISM; ENZYME STABILITY; PROTEIN CONFORMATION; PROTEIN DENATURATION; SPECTROMETRY, FLUORESCENCE; THERMODYNAMICS;

CARICA PAPAYA;

EID: 0037027955     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10234     Document Type: Article

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