Engineering of a monomeric and low-glycosylated form of human butyrylcholinesterase: Expression, purification, characterization and crystallization

European Journal of Biochemistry

Volumn 269, Issue 2, 2002, Pages 630-637

  Nachon, Florian ^a   Nicolet, Yvain ^b   Viguié, Nathalie ^a   Masson, Patrick ^a   Fontecilla Camps, Juan C ^b   Lockridge, Oksana ^c  

^a CENTRE DE RECHERCHES   (France)

^b INSTITUT DE BIOLOGIE STRUCTURALE   (France)

^c UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Butyrylcholinesterase; Crystallization; N glycosylation; Site directed mutagenesis; X ray diffraction

Indexed keywords

CHOLINESTERASE; MONOMER; RECOMBINANT ENZYME;

ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYST; CHO CELL; CONTROLLED STUDY; CRYSTAL STRUCTURE; CRYSTALLIZATION; DIFFRACTION; ENZYME ANALYSIS; ENZYME ENGINEERING; ENZYME MECHANISM; ENZYME PURIFICATION; ENZYME RELEASE; ENZYME STABILITY; GLYCOSYLATION; MOLECULAR SIZE; NONHUMAN; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN EXPRESSION; SOLUBILITY; STRUCTURE ANALYSIS; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; BUTYRYLCHOLINESTERASE; CATALYSIS; CRYSTALLIZATION; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOSYLATION; HUMANS; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN ENGINEERING; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; X-RAY DIFFRACTION;

ANIMALIA;

EID: 0036164151     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.0014-2956.2001.02692.x     Document Type: Article

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