Croatica Chemica Acta, Vol. 46 No. 2, 1974.
Izvorni znanstveni članak
Michaelis Constants and Substrate Inhibition Constants for the Reaction of Acetylthiocholine with Acetylcholinesterase and Cholinesterase
Vera Simeon
; Institute for Medical Research and Occupa.tional Health, Yugoslav Academy of Sciences and Arts, 41000 Zagreb, Croatia, Yugoslavia
Sažetak
The activity of erythrocyte acetylcholtnesterase at 5 °c and
25 °c and serum cholinesterase between 10 °C and 40 °c was
measured with acetylthiocholine as a substrate. Michaelis consta,rits
(Km) and substrate inhibition constants (Ks8
) were calculated. Km constants were calculated according to the Michaelis and Hill equations, while the Kss constants were assesed graphically from pS curves and also calculated acco,rding to the equation which takesinto account the hydrolysis of the enzyme-substrate inhibited complex. K ss constants and K
111 constants from the Hill equation weJ"e obtained at minimum x ~ value. Km and K 88 constants arealmost independent of temperature while the maximal activities increase with temperature. Energies of activation were calculated from these data.
Ključne riječi
Hrčak ID:
196828
URI
Datum izdavanja:
1.11.1974.
Posjeta: 700 *