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Inhibition of cholinesterases by bambuterol and haloxon (CROSBI ID 486024)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | domaća recenzija

Štuglin, Anita ; Latas, Tatjana ; Kovarik, Zrinka Inhibition of cholinesterases by bambuterol and haloxon // 1st Croatian Congress on Molecular Life Sciences with International Participation, Opatija, Book of Abstracts / Dumić, Jerka et al. (ur.). Zagreb: Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 2002. str. 125-x

Podaci o odgovornosti

Štuglin, Anita ; Latas, Tatjana ; Kovarik, Zrinka

engleski

Inhibition of cholinesterases by bambuterol and haloxon

Carbamates and organophosphorus compounds are potent inhibitors of serine esterases, butyrylcholinesterase (EC 3.1.1.8) and acetylcholinesterase (EC 3.1.1.7). To compare interaction of mouse acetylcholinesterase and butyrylcholinesterase, as well as those of butyrylcholinesterase from mouse, human, or horse, inhibition by bambuterol (5[2-(tert-butylamino)-1-hydroxyethyl]-m-phenylene-bis(dimethylcarbamate) hydrochloride) and haloxon (Di-(2-chloroethyl)-3-chloro-4-methyl-coumarin-7-yl phosphate) was performed. The time course of inhibition was followed by measuring the enzyme activity using spectrophotometric method, and the rate constants inhibition were calculated. Both inhibitors were faster inhibitor of butyrylcholinesterase from all studied species than of mouse acetylcholinesterase. Mouse butyrylcholinesterase is 16 000-times faster inhibited by bambuterol (ki (bambuterol)=5.7 x 106 min-1M-1) and 90-times by haloxon (ki (haloxon)=3.9 x 107 min-1M-1) than mouse acetylcholinesterase. Six aliphatic amino acids in active gorge of butyrylcholinesterase, which are in acetylcholinesterase substitute for six aromatic amino acids, provide better approach of bambuterol and haloxon to the catalytic centre of the enzyme resulting by more efficient inhibition of butyrylcholinesterase in comparison to acetylcholinesterase. The rate inhibition constants of horse butyrylcholinesterase differ about 25– times by bambuterol and about 4– times by haloxon from the rates of mouse or human butyrylcholinesterase. Similar inhibition rates of mouse and human butyrylcholinesterase are dictated by higher amino acid sequence homology than that of horse butyrylcholinesterase. Primarily structure of horse butyrylcholinesterase differs from the sequences of the other two species in six amino acids.

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Podaci o prilogu

125-x.

2002.

objavljeno

Podaci o matičnoj publikaciji

1st Croatian Congress on Molecular Life Sciences with International Participation, Opatija, Book of Abstracts

Dumić, Jerka et al.

Zagreb: Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu

Podaci o skupu

1 st Croatian congress on molecular life sciences with international participation

poster

09.06.2002-13.06.2002

Opatija, Hrvatska

Povezanost rada

Temeljne medicinske znanosti