L-Arginine increases the solubility of unfolded species of hen egg white lysozyme

Protein Science

Volumn 14, Issue 4, 2005, Pages 929-935

  Reddy K , Ravi Charan ^a   Lilie, Hauke ^b   Rudolph, Rainer ^b   Lange, Christian ^b  

^a BANARAS HINDU UNIVERSITY   (India)

^b MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

Author keywords

Aggregation; L arginine; Lysozyme; Refolding

Indexed keywords

ARGININE; CYSTEINE; EGG WHITE; LYSOZYME;

ARTICLE; CHEMICAL MODIFICATION; CONTROLLED STUDY; DIFFERENTIAL SCANNING CALORIMETRY; EGG; ENZYME ACTIVITY; MODEL; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN RENATURATION; SOLUBILITY;

ARGININE; KINETICS; MURAMIDASE; PROTEIN FOLDING; PROTEIN RENATURATION; SOLUBILITY;

EID: 15244343628     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.041085005     Document Type: Article

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