Parallel mechanisms in acetylcholinesterase-catalyzed hydrolysis of choline esters

1993 ◽  
Vol 115 (23) ◽  
pp. 10477-10482 ◽  
Author(s):  
Trevor Selwood ◽  
Shawn R. Feaster ◽  
Michael J. States ◽  
Alton N. Pryor ◽  
Daniel M. Quinn
Keyword(s):  
Parallel Mechanisms ◽  
Choline Esters ◽  
Hydrolysis Of

HYDROLYSIS OF CHOLINE ESTERS IN THE PRESENCE OF ADRENALIN

1949 ◽  
Vol 158 (3) ◽  
pp. 327-331 ◽  
Author(s):  
Wilbur M. Benson ◽  
Walter J. Meek
Keyword(s):  
Choline Esters ◽  
Hydrolysis Of

THE ACTION OF NORMAL AND ATYPICAL CHOLINESTERASE OF HUMAN SERUM UPON A SERIES OF ESTERS OF CHOLINE

1960 ◽  
Vol 38 (6) ◽  
pp. 545-551 ◽  
Author(s):  
R. O. Davies ◽  
A. V. Marton ◽  
W. Kalow
Keyword(s):  
Normal Type ◽  
Choline Esters ◽  
Different Types ◽  
Human Sera ◽  
Michaelis Constants ◽  
Normal Enzyme ◽  
Atypical Cholinesterase ◽  
Hydrolysis Of ◽  
Individual Human ◽  
Support Evidence

The results of a comparison of the actions of individual human sera support evidence previously obtained for the existence of two different types of pseudocholinesterase in man. Maximum rates of hydrolysis of choline esters by human sera containing the normal type of cholinesterase were two to four times greater than the maximum rates obtained with sera containing atypical esterase. Human sera with the normal type of cholinesterase hydrolyzed butyrylcholine at a considerably faster rate than pentanoylcholine; atypical esterase hydrolyzed pentanoylcholine at approximately the same rate as butyrylcholine. All Michaelis constants for the normal enzyme were lower than those for the atypical enzyme by a factor which varied from 1.4 to 6.4. The data were compatible with the assumption of a linear relationship between the log of the Michaelis constants and the number of acyl carbons in the choline esters, but the slopes differed significantly for the two enzymes. For a homologous series of choline esters, there was no correlation between rates of hydrolysis and Michaelis constants.

scholarly journals The Hydrolysis of Some Choline Esters.

1954 ◽  
Vol 8 ◽  
pp. 1017-1020 ◽  
Author(s):  
Lennart Larsson ◽  
John McPherson ◽  
W. E. Harvey ◽  
Nils Andreas Sörensen
Keyword(s):  
Choline Esters ◽  
Hydrolysis Of

Hydrolysis of choline esters of N-substituted amino acids under the action of butyrylcholinesterase

1984 ◽  
Vol 18 (7) ◽  
pp. 453-457 ◽  
Author(s):  
V. O. Topuzyan ◽  
G. P. Alebyan ◽  
O. L. Mndzhoyan
Keyword(s):  
Amino Acids ◽  
Choline Esters ◽  
Hydrolysis Of

HYDROLYSIS OF CHOLINE ESTERS BY LIVER

Science ◽  
1945 ◽  
Vol 101 (2624) ◽  
pp. 385-386 ◽  
Author(s):  
C. H. SAWYER
Keyword(s):  
Choline Esters ◽  
Hydrolysis Of

On the active site for hydrolysis of aryl amides and choline esters by human cholinesterases

2006 ◽  
Vol 14 (13) ◽  
pp. 4586-4599 ◽  
Author(s):  
Sultan Darvesh ◽  
Robert S. McDonald ◽  
Katherine V. Darvesh ◽  
Diane Mataija ◽  
Sam Mothana ◽  
...  
Keyword(s):  
Active Site ◽  
Choline Esters ◽  
Hydrolysis Of

scholarly journals Comparison between the Acetylcholinesterases of Helix Blood and Cobra Venom. II. The Hydrolysis of Certain Choline and Non-Choline Esters.

1951 ◽  
Vol 5 ◽  
pp. 712-723 ◽  
Author(s):  
Klas-Bertil Augustinsson ◽  
R. K. Bonnichsen ◽  
D. I. Arnon ◽  
Jörgine Stene Sörensen ◽  
Nils Andreas Sörensen
Keyword(s):  
Cobra Venom ◽  
Choline Esters ◽  
Hydrolysis Of

scholarly journals Comparison of Two Storage Methods for the Analysis of Cholinesterase Activities in Food Animals

2010 ◽  
Vol 2010 ◽  
pp. 1-11 ◽  
Author(s):  
Kasim Abass Askar ◽  
A. Caleb Kudi ◽  
A. John Moody
Keyword(s):  
Significant Inhibition ◽  
Mean Difference ◽  
Altman Plot ◽  
Choline Esters ◽  
Cholinesterase Activities ◽  
The Mean ◽  
Storage Methods ◽  
Lower Limits ◽  
Hydrolysis Of

Cholinesterases (ChE) are specialized carboxylic ester hydrolases that catalyse the hydrolysis of choline esters. They are classified into either acetylcholinesterase (AChE) or butyrylcholinesterase (BChE). Determination of ChE in the tissues is the appropriate tool for the diagnosis of organophosphorus and carbamate exposures. In general, a significant inhibition was seen in both AChE and BChE activities after 6 months of freezing at −80°C and after 3 months of freezing at −20°C. Linear regression of mean AChE and BChE was observed in all individual samples during the months of the two freezing methods. Bland and Altman plot of the ratios of the two freezing methods have showen the mean difference between the two freezing methods to be 8.8, and SD was 144.7 and −127.6 for upper and lower limits, respectively, for liver, while in muscle the mean difference was 1.5 and SD was 32.5 and −28.9 for upper and lower limits, respectively.

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