The xanthine oxidase and its associated activities in the ovine milk and liver: distinctive in impact of in vivo molybdenum
Mukhamejanova, Akmaral | Alikulov, Zerekbay | Tuganova, Bakyt | Adamzhanova, Zhanna
Xanthine oxidase is molybdenum and iron-containing flavoprotein, catalyzing the final oxidation stage of purines and oxidative transformation of pterins and some aliphatic and aromatic aldehydes. Despite the importance of this enzyme, the distribution of xanthine oxidase in traditional household animal’s milk and tissues is unknown. Formerly, we have found most of the xanthine oxidase molecules in animal milk are inactive because of a lack of molybdenum. Ovine milk was processed by inserting in vivo molybdenum (tungsten) into drinking water. We gave opposite dates in the presence of tungsten too. Heating the milk of animals at 80 °C for 5 minutes in the presence of molybdenum and cysteine led to a sharp increase of xanthine oxidase and its associated – nitrate reductase and nitrite reductase activities. The change of xanthine oxidase and its associated activities were examined by spectrophotometry after treatment. It was established that metal ions added in drinking water for animals have an impact on enzyme activities. The activity is formed in the ovine liver even in the absence of exogenous molybdenum in drinking water. The associated activities of liver enzymes in the presence of molybdenum in drinking water had slightly increased. Tungsten-containing water led to the loss of all activities of liver xanthine oxidase. It is proposed that the liver contains a special protein involving in the incorporation of molybdenum (or tungsten) into xanthine oxidase molecule, however, the milk or mammary gland compounds lack this protein.
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