Catalytic properties of human serum esterases hydrolysing paraoxon and phenylacetate (CROSBI ID 470132)
Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija
Podaci o odgovornosti
Reiner, Elsa
engleski
Catalytic properties of human serum esterases hydrolysing paraoxon and phenylacetate
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.
human serum esterases; paraoxon; phenylacetate
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Podaci o prilogu
L1-x.
1998.
objavljeno
Podaci o matičnoj publikaciji
Glavaš-Obrovac, Ljubica
Zagreb: Farmaceutsko-biokemijski fakultet Sveučilišta u Zagrebu
Podaci o skupu
Annual Meeting of Croatian Biochemists with International Participation
pozvano predavanje
17.09.1998-20.09.1998
Bizovac, Hrvatska