Exploring the structural and functional stabilities of different paraoxonase-1 formulations through electrophoretic mobilities and enzyme activity parameters under hydrostatic pressure

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1794, Issue 4, 2009, Pages 680-688

  Cléry Barraud, Cécile ^a   Renault, Frédérique ^a   Leva, Julien ^a   El Bakdouri, Nacéra ^a   Masson, Patrick ^a   Rochu, Daniel ^a,b  

^a CENTRE DE RECHERCHES   (France)

^b BUNDESWEHR INSTITUTE OF PHARMACOLOGY AND TOXICOLOGY   (Germany)

Author keywords

Functional stability; High hydrostatic pressure; Human phosphate binding protein; Oligomerization; Paraoxonase; Stability

Indexed keywords

ARYLDIALKYLPHOSPHATASE 1; HIGH DENSITY LIPOPROTEIN; PHOSPHATE BINDING PROTEIN;

ARTICLE; CONTROLLED STUDY; ELECTROPHORETIC MOBILITY; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME STABILITY; ENZYME STRUCTURE; HUMAN; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN POLYMERIZATION;

ARYLDIALKYLPHOSPHATASE; ELECTROPHORESIS, CAPILLARY; HUMANS; HYDROSTATIC PRESSURE; KINETICS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; THERMODYNAMICS;

EID: 61649108075     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2009.01.003     Document Type: Article

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