Pressure and heat inactivation of recombinant human acetylcholinesterase: Importance of residue E202 for enzyme stability

European Journal of Biochemistry

Volumn 269, Issue 17, 2002, Pages 4297-4307

  Cléry Barraud, Cécile ^a,c   Ordentlich, Arie ^b   Grosfeld, Haim ^b   Shafferman, Avigdor ^b   Masson, Patrick ^a  

^a Centre de Recherches du Service de Sante des Armees   (France)

^b ISRAEL INSTITUTE FOR BIOLOGICAL RESEARCH   (Israel)

^c CENTRE DE RECHERCHES   (France)

Author keywords

Acetylcholinesterase; Inactivation; Mutants; Pressure; Protein stability

Indexed keywords

8 ANILINO 1 NAPHTHALENESULFONIC ACID; ACETYLCHOLINESTERASE; AMINO ACID; CARBOXYL GROUP; MUTANT PROTEIN;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME INACTIVATION; ENZYME STABILITY; ENZYME STRUCTURE; EXPOSURE; FLUORESCENCE; GEL ELECTROPHORESIS; GENE MUTATION; HEAT TREATMENT; HUMAN; HYDROSTATIC PRESSURE; PRIORITY JOURNAL; PROTEIN FUNCTION; SURFACE CHARGE; TEMPERATURE SENSITIVITY; THERMOSTABILITY;

ACETYLCHOLINESTERASE; BINDING SITES; CELLS, CULTURED; ENZYME STABILITY; FLUORESCENCE; HEAT; HUMANS; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NAPHTHALENESULFONATES; PRESSURE; PROTEIN CONFORMATION; PROTEIN DENATURATION; RECOMBINANT PROTEINS; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 0036042537     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1033.2002.03122.x     Document Type: Article

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