Monitoring the reaction of carbachol with acetylcholinesterase by thioflavin T fluorescence and acetylthiocholine hydrolysis

Chemico-Biological Interactions

Volumn 175, Issue 1-3, 2008, Pages 235-241

  Rosenberry, Terrone L ^a   Sonoda, Leilani K ^a   Dekat, Sarah E ^a   Cusack, Bernadette ^a   Johnson, Joseph L ^a  

^a MAYO CLINIC   (United States)

Author keywords

Acetylcholinesterase; Carbamoylation; Enzyme mechanism; Peripheral site; Thioflavin T

Indexed keywords

ACETYLCHOLINE; ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; CARBACHOL; CHOLINESTERASE INHIBITOR; RECOMBINANT ENZYME; THIOFLAVINE;

ACYLATION; ALZHEIMER DISEASE; ARTICLE; BINDING AFFINITY; BINDING SITE; CARBAMOYLATION; CATALYSIS; CHEMICAL REACTION; DEACYLATION; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; FLUORESCENCE; HYDROLYSIS; LIGAND BINDING; STEADY STATE; ULTRAVIOLET SPECTROPHOTOMETRY;

ACETYLCHOLINESTERASE; ACETYLTHIOCHOLINE; CARBACHOL; HUMANS; HYDROLYSIS; RECOMBINANT PROTEINS; SPECTROMETRY, FLUORESCENCE; THIAZOLES;

EID: 50649109814     PISSN: 00092797     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbi.2008.06.002     Document Type: Article

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