hrcak mascot   Srce   HID

Izvorni znanstveni članak

Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon

Zrinka Kovarik   ORCID icon orcid.org/0000-0001-9863-886X ; Institute for Medical Research and Occupational Health, Ksaverska c. 2, POB 291, HR-10001 Zagreb, Croatia
Anita Bosak   ORCID icon orcid.org/0000-0003-0164-4994 ; Institute for Medical Research and Occupational Health, Ksaverska c. 2, POB 291, HR-10001 Zagreb, Croatia
Goran Šinko ; Institute for Medical Research and Occupational Health, Ksaverska c. 2, POB 291, HR-10001 Zagreb, Croatia
Tatjana Latas ; Institute for Medical Research and Occupational Health, Ksaverska c. 2, POB 291, HR-10001 Zagreb, Croatia

Puni tekst: engleski, pdf (364 KB) str. 63-67 preuzimanja: 684* citiraj
APA 6th Edition
Kovarik, Z., Bosak, A., Šinko, G. i Latas, T. (2003). Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon. Croatica Chemica Acta, 76 (1), 63-67. Preuzeto s https://hrcak.srce.hr/103058
MLA 8th Edition
Kovarik, Zrinka, et al. "Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon." Croatica Chemica Acta, vol. 76, br. 1, 2003, str. 63-67. https://hrcak.srce.hr/103058. Citirano 09.03.2021.
Chicago 17th Edition
Kovarik, Zrinka, Anita Bosak, Goran Šinko i Tatjana Latas. "Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon." Croatica Chemica Acta 76, br. 1 (2003): 63-67. https://hrcak.srce.hr/103058
Harvard
Kovarik, Z., et al. (2003). 'Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon', Croatica Chemica Acta, 76(1), str. 63-67. Preuzeto s: https://hrcak.srce.hr/103058 (Datum pristupa: 09.03.2021.)
Vancouver
Kovarik Z, Bosak A, Šinko G, Latas T. Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon. Croatica Chemica Acta [Internet]. 2003 [pristupljeno 09.03.2021.];76(1):63-67. Dostupno na: https://hrcak.srce.hr/103058
IEEE
Z. Kovarik, A. Bosak, G. Šinko i T. Latas, "Exploring the Active Sites of Cholinesterases by Inhibition with Bambuterol and Haloxon", Croatica Chemica Acta, vol.76, br. 1, str. 63-67, 2003. [Online]. Dostupno na: https://hrcak.srce.hr/103058. [Citirano: 09.03.2021.]

Sažetak
The paper describes the inhibition of mouse acetylcholinesterase (AChE; EC 3.1.1.7) and mouse, human, and horse butyrylcholinesterase (BChE; EC 3.1.1.8) by 5-[2-(tert-butylamino)-1-hydroxyethyl]-m-phenylene-bis(dimethylcarbamate) hydrochloride (bambuterol) and by O,O-bis-(2-chloroethyl)-O-(3-chloro-4-methylcoumarin-7-yl) phosphate (haloxon). The haloxon inhibition rate constant (ki) for mouse BChE was 3.7 × 107 min–1 mol–1 dm3, which was 40-fold higher than the rate constant for mouse AChE. Bambuterol inhibition of horse BChE (ki = 2.1 × 105 min–1 mol–1 dm3) was about 25-fold slower than that of human or mouse BChE, whereas the respective haloxon inhibition of horse BChE (ki = 1.2 × 107 min–1 mol–1 dm3) was about 2-3-fold slower. Sequence alignments and the computational model of the three-dimensional structure of horse BChE suggest that residues inside the active site at positions 69, 277 and 285 are important for the differences in the inhibition of these three BChE species.

Ključne riječi
mouse acetylcholinesterase; mouse, human and horse butyrylcholinesterase; inhibition; carbamate; organophosphate; haloxon; bambuterol

Hrčak ID: 103058

URI
https://hrcak.srce.hr/103058

Posjeta: 889 *