TITLE

SULFATO, CHLORIDO, CINKO IR KADMIO JONŲ POVEIKIS 5-AMINOLEVULINO RŪGŠTIES DEHIDRATAZĖS AKTYVUMUI BANDOMŲJŲ GYVŪNŲ KRAUJYJE in vitro

AUTHOR(S)
Ryselis, Stanislovas; Baranauskienė1, Dalė; Abdrachmanovas, Olegas; Naginienė1,, Rima; Stepaniukas, Andrius; Šernienė, Loreta
PUB. DATE
September 2007
SOURCE
Veterinarija ir Zootechnika;2007, Vol. 39 Issue 61, p53
SOURCE TYPE
Academic Journal
DOC. TYPE
Article
ABSTRACT
In the present reseach the influence of zinc ions (Zn2+) on the activity of 5-aminoleavulinic acid dehydratase (5-ALAD) in blood in vitro upon impact of cadmium (Cd2+), sulphate (SO42-) and chloride (Cl-) ions was investigated. The obtained curves of the consecutive multidot dependences and Cd2+ concentrations causing half-maximal inhibition (IC50*) showed that Cd2+ inhibited the activity of enzyme 5-ALAD in vitro in higher extent compared to equimolar concentrations of Zn2+. In comparison to Zn2+ the leap of enzymes activity inhibition and IC50 occurred under the lower concentrations of Cd2+. Reduced concentrations of SO42- and Cl- increased the 5-ALAD activity penetrating its maximumes, while high concentrations of SO42- and Cl- decreased the activity of enzyme, but not inhibited the enzymes activity. The shift of the leap and IC50 of the inhibition of 5-ALAD activity under the impact of Cd2+ ions inhibited the enzyme later in precence of Zn2+ additions and lower compared to natural concentration of Zn2+. aAlthough Zn2+ ions are characterized by the low protective activity in vitro. The investigations showed that the effects of SO42-, Cl-, Zn2+ and Cd2+ ions on blood 5-ALAD activity can be predicted, compared and evaluated in vitro according to the impulse of the leap of enzyme inhibition (concentration value of the catalytic poison, which cause half-maximal inhibition - IC50).
ACCESSION #
27157151

 

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