Malathion-induced inhibition of human plasma cholinesterase studied by the fluorescence spectroscopy method

2008 ◽  
Vol 82 (5) ◽  
pp. 870-874 ◽  
Author(s):  
V. M. Pavelkić ◽  
K. S. Krinulović ◽  
J. Z. Savić ◽  
M. A. Ilić
2000 ◽  
Vol 14 (1) ◽  
pp. 30-34 ◽  
Author(s):  
Masato Kato ◽  
Yasuhiko Hashimoto ◽  
Takashi Horinouchi ◽  
Taishi Ando ◽  
Jun Ito ◽  
...  

1970 ◽  
Vol 47 (2) ◽  
pp. 177-182 ◽  
Author(s):  
MARY WHITTAKER

SMUMARY Concentrations of thyroxine above 10-7m inhibited the activity of the 'usual' and 'atypical' human plasma cholinesterase in vitro. The 'atypical' enzy mewas more readily inhibited and the ratio of the I50 atypical: I50 usual indicates that the hormone can be used as a differential inhibitor to identify the two phenotypes. Similar results were obtained with thiourea, but the action of thiouracil appeared to differ in so far as this inhibited both enzymes to the same extent. Neither glucagon nor thyroid stimulating hormone had any effect.


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