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<b:Sources SelectedStyle="" xmlns:b="http://schemas.openxmlformats.org/officeDocument/2006/bibliography"  xmlns="http://schemas.openxmlformats.org/officeDocument/2006/bibliography" >
<b:Source>
<b:Tag>cjs-202305-0003</b:Tag>
<b:SourceType>ArticleInAPeriodical</b:SourceType>
<b:Year>2023</b:Year>
<b:PeriodicalName>Czech Journal of Animal Science</b:PeriodicalName>
<b:Volume>68</b:Volume>
<b:Issue>5</b:Issue>
<b:Pages>222-230</b:Pages>
<b:Author>
<b:Author><b:NameList>
<b:Person><b:Last>Aubakirova</b:Last><b:First>Karlygash</b:First></b:Person>
<b:Person><b:Last>Satkanov</b:Last><b:First>Mereke</b:First></b:Person>
<b:Person><b:Last>Kulataeva</b:Last><b:First>Maral</b:First></b:Person>
<b:Person><b:Last>Assylbekova</b:Last><b:First>Gulmira</b:First></b:Person>
<b:Person><b:Last>Kambarbekova</b:Last><b:First>Aigul</b:First></b:Person>
<b:Person><b:Last>Alikulov</b:Last><b:First>Zerekbai</b:First></b:Person>
</b:NameList></b:Author>
</b:Author>
<b:Title>Molybdoenzymes isolated from S. glanis liver can produce nitric oxide from nitrates and nitrites</b:Title>
<b:Comments>Nitric oxide (NO) plays numerous essential physiological functions in&#160;terrestrial animals. In&#160;mammals, NO production from l-arginine is catalysed by&#160;the enzyme NO synthase (NOS). In&#160;recent years, data have begun to&#160;emerge on NOS expression and the physiological significance of&#160;NO in&#160;ectothermic vertebrates such as&#160;fish. However, there are relatively fewer data compared to&#160;the mammalian system. Although it is already well known that animal molybdoenzymes can convert nitrate and nitrite into NO, there is almost no information on the content and properties of&#160;molybdoenzymes in&#160;fish organs in&#160;the scientific literature. In&#160;this regard, the objectives of&#160;the present work were to&#160;detect the activity of&#160;classical molybdoenzymes xanthine oxidase (XO) and aldehyde oxidase (AO) in&#160;the liver and to&#160;study their possible activity to&#160;reduce nitrate and nitrite to&#160;nitrogen monoxide. In&#160;this work, the intrinsic activity of&#160;XO and AO was examined by&#160;using their substrates. At&#160;the same time, their nitrate (NR) - and nitrite reductase (NiR) activity were determined. It was determined that&#160;XO and AO in&#160;the fish liver are mainly represented by&#160;the molybdenum-free forms. The presence of&#160;an additional source of&#160;molybdenum can activate both the intrinsic and the&#160;NR and NiR activities. The NiR activity of&#160;XO and AO was higher than their NR activity. The data shows that treatment at&#160;a&#160;concentration of&#160;sodium molybdate and glutathione of&#160;1.0 mM increases all activities of&#160;XO and AO. The optimal conditions for maximum activation of&#160;exogenous molybdate for&#160;XO and AO were reached by&#160;heating at&#160;70 &#176;C for&#160;5 minutes. The activity of&#160;XO increased almost 4.7 times, and the activity of&#160;AO 7.7 times compared with its intrinsic activity without heat treatment. NO is formed from nitrite by&#160;the enzymes XO and AO much more than from nitrate.</b:Comments>
</b:Source>
</b:Sources>
