The butyrylcholinesterase K-variant shows similar cellular protein turnover and quaternary interaction to the wild-type enzyme

Journal of Neurochemistry

Volumn 74, Issue 2, 2000, Pages 869-877

  Altamirano, Cibby Varkey ^a   Bartels, Cynthia F ^a   Lockridge, Oksana ^a,b  

^a UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

Author keywords

Butyrylcholinesterase; K variant; Late onset Alzheimer's disease

Indexed keywords

CHOLINESTERASE; ENZYME VARIANT;

ALZHEIMER DISEASE; ANIMAL CELL; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENZYME ACTIVITY; ENZYME PURIFICATION; GENE MUTATION; HYDROLYSIS; NEUROFIBRILLARY TANGLE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN METABOLISM; PROTEIN PROTEIN INTERACTION;

ADULT; ANIMALS; BUTYRYLCHOLINESTERASE; CATALYSIS; CHO CELLS; CRICETINAE; FEMALE; GENE FREQUENCY; HUMANS; MALE; MUTATION; PROTEIN STRUCTURE, QUATERNARY; VARIATION (GENETICS);

EID: 0033971911     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.740869.x     Document Type: Article

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