Mechanism for stabilization of the molten globule state of papain by sodium n-alkyl sulfates: Spectroscopic and calorimetric approaches

Journal of Colloid and Interface Science

Volumn 322, Issue 1, 2008, Pages 119-127

  Chamani, J ^a   Heshmati, M ^a  

^a ISLAMIC AZAD UNIVERSITY   (Iran)

Author keywords

Aggregation; Hydrophobic interactions; Molten globule state; Papain; Sodium n alkyl sulfates; Stabilization

Indexed keywords

AGGLOMERATION; CALORIMETRY; DICHROISM; FLUORESCENCE; HYDROPHOBICITY; SODIUM COMPOUNDS; STABILIZATION;

HYDROPHOBIC INTERACTIONS; MOLTEN GLOBULE STATE; SODIUM N-ALKYL SULFATES; SUBSTANTIAL VARIATIONS;

PROTEINS;

ALKANESULFONIC ACID; BUFFER; GUANIDINE; PAPAIN;

ARTICLE; CIRCULAR DICHROISM; CONCENTRATION (PARAMETERS); DIFFERENTIAL SCANNING CALORIMETRY; FLUORESCENCE; HYDROPHOBICITY; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN FOLDING; PROTEIN STABILITY; TEMPERATURE;

CALORIMETRY, DIFFERENTIAL SCANNING; DRUG STABILITY; HYDROGEN-ION CONCENTRATION; HYDROPHOBICITY; KINETICS; PAPAIN; PROTEIN FOLDING; SODIUM; SPECTROPHOTOMETRY, ULTRAVIOLET; SULFURIC ACID ESTERS; THERMODYNAMICS;

EID: 43049119004     PISSN: 00219797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jcis.2008.03.001     Document Type: Article

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