The prominent conformational plasticity of lactoperoxidase: A chemical and pH stability analysis

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 7, 2009, Pages 1041-1048

  Boscolo, Barbara ^a   Leal, Sónia S ^b   Salgueiro, Carlos A ^c   Ghibaudi, Elena M ^a   Gomes, Cláudio M ^b  

^a UNIVERSITY OF TURIN   (Italy)

^b INSTITUTO DE TECNOLOGIA QUÍMICA E BIOLÓGICA   (Portugal)

^c DEPARTAMENTO DE QUÍMICA   (Portugal)

Author keywords

Chemical denaturation; Heme protein; Mammalian peroxidase; pH effect; Protein folding; Structural stability

Indexed keywords

GUANIDINE; HEME; LACTOPEROXIDASE; UREA;

ARTICLE; CHEMICAL INTERACTION; CONFORMATION; CONTROLLED STUDY; DENATURATION; ELECTRON SPIN RESONANCE; ENZYME ACTIVITY; ENZYME STABILITY; ENZYME STRUCTURE; FLUORESCENCE; NONHUMAN; PH; PRIORITY JOURNAL; PROTEIN BINDING;

ELECTRON SPIN RESONANCE SPECTROSCOPY; ENZYME STABILITY; HEME; HYDROGEN-ION CONCENTRATION; LACTOPEROXIDASE; PROTEIN CONFORMATION; PROTEIN DENATURATION; STATIC ELECTRICITY;

MAMMALIA;

EID: 67349089554     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.03.003     Document Type: Article

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