Association of tetramers of human butyrylcholinesterase is mediated by conserved aromatic residues of the carboxy terminus

Chemico-Biological Interactions

Volumn 119-120, Issue , 1999, Pages 53-60

  Altamirano, Cibby Varkey ^a   Lockridge, Oksana ^a  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Butyrylcholinesterase; K variant; Poly L proline; Proline rich attachment domain; Tetramerization domain; Yeast two hybrid system

Indexed keywords

ACETYLCHOLINESTERASE; CHOLINESTERASE; ORGANOPHOSPHATE; PROLINE DERIVATIVE; TETRAMER;

ANIMAL CELL; ANIMAL TISSUE; CELL STRAIN COS1; CONFERENCE PAPER; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME MODIFICATION; ENZYME STABILITY; ENZYME STRUCTURE; MUTANT; NONHUMAN; PROTEIN DOMAIN; PROTEIN EXPRESSION; RAT; YEAST;

AMINO ACID SEQUENCE; ANIMALS; BUTYRYLCHOLINESTERASE; CATS; CATTLE; CHICKENS; CONSERVED SEQUENCE; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTATION; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RABBITS; RATS; SEQUENCE HOMOLOGY, AMINO ACID; TORPEDO;

EID: 18744437671     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0009-2797(99)00013-7     Document Type: Conference Paper

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