Nalazite se na CroRIS probnoj okolini. Ovdje evidentirani podaci neće biti pohranjeni u Informacijskom sustavu znanosti RH. Ako je ovo greška, CroRIS produkcijskoj okolini moguće je pristupi putem poveznice www.croris.hr
izvor podataka: crosbi

Quantification of butyrylcholinesterase active sites in purified preparations using organophosphorus compounds (CROSBI ID 100207)

Prilog u časopisu | izvorni znanstveni rad | međunarodna recenzija

Kovarik, Zrinka ; Latas, Tatjana ; Simeon-Rudolf, Vera Quantification of butyrylcholinesterase active sites in purified preparations using organophosphorus compounds // Periodicum biologorum, 104 (2002), 4; 481-485-x

Podaci o odgovornosti

Kovarik, Zrinka ; Latas, Tatjana ; Simeon-Rudolf, Vera

engleski

Quantification of butyrylcholinesterase active sites in purified preparations using organophosphorus compounds

Background and purpose: The inhibition of butyrylcholinesterase (BChE ; EC 3.1.1.8) by covalently binding inhibitors such as organophosphorus compounds makes it possible to determine the quantity of the enzyme active sites in samples. This approach is applicable only if the phosphorylated enzyme conjugate is stable. The kinetics of interaction of horse serum BChE with DEPQ (7-(O, O-diethylphosphinyloxy)-1-methylquinolinium methyl sulphate) and haloxon (O, O-di-(2-chloroethyl)-O-(3-chloro-4-methylcoumarin-7-yl) phosphate) was studied in order to evaluate whether these compounds were suitable for quantification of active sites in a commercial preparation of horse serum BChE. Materials and methods: The BChE preparation was inhibited by haloxon and DEPQ, and the inhibition rate constants were calculated. The rate constant of spontaneous reactivation of BChE phosphorylated by haloxon was determined. Stoichiometric subnanomolar concentrations of the inhibitor and enzyme were used for the quantification of the active sites. The enzyme activity was measured spectrophotometricaly using acetylthiocholine as the substrate. Results and conclusions

DEPQ; haloxon; active site titration; inhibition; cholinesterase

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

nije evidentirano

Podaci o izdanju

104 (4)

2002.

481-485-x

objavljeno

0031-5362

Povezanost rada

Kemija

Indeksiranost