pH dependence of the activation parameters for chymopapain unfolding: Influence of ion pairs on the kinetic stability of proteins

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1388, Issue 2, 1998, Pages 363-372

  Solís Mendiola, Silvia ^a   Gutiérrez González, Luis H ^a   Arroyo Reyna, Alfonso ^a   Padilla Zúñiga, Jacqueline ^a   Rojo Domínguez, Arturo ^a   Hernández Arana, Andrés ^a  

^a DEPARTAMENTO DE QUÍMICA   (Mexico)

Author keywords

Activation parameter; Ion pair; pH effect; Unfolding kinetics

Indexed keywords

CHYMOPAPAIN; LYSOZYME; TRYPSIN;

ARTICLE; ENTHALPY; ENTROPY; PH; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY;

CHYMOPAPAIN; CIRCULAR DICHROISM; CYSTEINE ENDOPEPTIDASES; ENZYME ACTIVATION; ENZYME STABILITY; HYDROGEN-ION CONCENTRATION; KINETICS; PLANT PROTEINS; PROTEIN DENATURATION; PROTEIN FOLDING; PROTONS; THERMODYNAMICS;

EID: 0032506293     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(98)00195-2     Document Type: Article

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