Modification of lysine residues of horseradish peroxidase and its effect on stability and structure of the enzyme

Applied Biochemistry and Biotechnology

Volumn 172, Issue 7, 2014, Pages 3558-3569

  Hassani, Leila ^a   Nourozi, Rasool ^a  

^a INSTITUTE FOR ADVANCED STUDIES IN BASIC SCIENCES IASBS   (Iran)

Author keywords

2,3 Dichloromaleic anhydride; 2,3 Dimethylmaleic anhydride; Chemical modification; Horseradish peroxidase; Spectroscopy

Indexed keywords

ACTIVATION ENERGY; ALKALINITY; AMINO ACIDS; CHEMICAL MODIFICATION; ENZYMES; METABOLISM; SPECTROSCOPY; STRUCTURE (COMPOSITION); THERMODYNAMIC STABILITY; UREA;

2,3-DICHLOROMALEIC ANHYDRIDE; 2,3-DIMETHYLMALEIC ANHYDRIDE; CATALYTIC EFFICIENCIES; DENATURING CONDITIONS; HORSE-RADISH PEROXIDASE; OXIDATIVE CONDITIONS; SPECTROSCOPIC TECHNIQUE; STRUCTURAL INVESTIGATION;

CHEMICAL STABILITY;

HORSERADISH PEROXIDASE; LYSINE;

CHEMISTRY; ENZYME STABILITY; GENETICS; KINETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN MOTIF; PROTEIN STABILITY;

AMINO ACID MOTIFS; ENZYME STABILITY; HORSERADISH PEROXIDASE; KINETICS; LYSINE; PROTEIN CONFORMATION; PROTEIN STABILITY;

EID: 84899414760     PISSN: 02732289     EISSN: 15590291     Source Type: Journal    
DOI: 10.1007/s12010-014-0756-y     Document Type: Article

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