Naslov
Catalytic properties of human serum esterases hydrolysing paraoxon and phenylacetate

Autori
Reiner, Elsa

Vrsta, podvrsta i kategorija rada
Sažeci sa skupova, sažetak, znanstveni

Izvornik
Godišnji sastanak hrvatskih biokemičara, Bizovačke Toplice, Sažeci znanstvenih priopćenja,ISBN 953-6256-28-2 / Glavaš-Obrovac, Ljubica - Zagreb : Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu, 1998

Skup
Annual Meeting of Croatian Biochemists with International Participation

Mjesto i datum
Bizovac, Hrvatska, 17.09.1998. - 20.09.1998

Vrsta sudjelovanja
Pozvano predavanje

Vrsta recenzije
Međunarodna recenzija

Ključne riječi
human serum esterases; paraoxon; phenylacetate

Sažetak
The organophosphorus compound paraoxon (POX) is the characteristic substrate of paraoxonase (EC 3.8.1.1) and phenylacetate (PA) is the characteristic substrate of arylesterase (EC 3.1.1.2). Mammalian sera contain EDTA-sensitive and the EDTA-insensitive esterases which hydrolyse POX , and the same applies to the hydrolysis of PA. It was shown that the EDTA insensitive hydrolysis of PA is not due to an arylesterase, but to a serine esterase, and it seems that the EDTA-sensitive hydrolysis of PA might be due to two esterases. The EDTA-sensitive and EDTA-insensitive hydrolysis of POX are probably both due to enzymes of the phoshoric triester hydrolase group (EC 3.8.1). Finnaly, it was shown that rates of POX and PA hydrolysis in human sera are affected by lipid and/or glucose metabolism disorders, which is particularly reflected in the EDTA-insensitive activities.

Izvorni jezik
Engleski

Znanstvena područja
Kliničke medicinske znanosti

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