The Distribution of the Enzyme Arginase in the Tissues of Selected Cichlidae Species: &lt;i&gt;Tilapia zillii, Sarotherodon galilaeus&lt;/i&gt; and &lt;i&gt;Oreochromis niloticus&lt;/i&gt;

Okonji, RE; Popoola, MO; Komolafe, OO; Kuku, Adenike

doi:10.4314/wajae.v18i1.70318

Cited by 2 publications

(4 citation statements)

References 26 publications

(21 reference statements)

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“…In this study, Oryctes rhinoceros larva arginase was purified with a specific activity of 38.7 U/mg, yield of 16.5%, and purification fold of 63.4. The specific activity of arginase as determined by different researchers varied from 5.21 to 40 U/mg protein (Okonji et al, 2011;Al-Saad et al, 2021). Okonji et al (2013) reported a specific activity of 3.7 U/mg of protein for grasshopper gut arginase.…”

Section: Discussionmentioning

confidence: 99%

Biochemical characterization of a purified arginase from the gut of Oryctes rhinoceros larvae

Famakinwa¹,

Itakorode²,

Adedeji³

et al. 2023

ijs

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Arginase acts as a mediator in the final phase of the urea cycle, protecting against excessive ammonia under homeostatic conditions by producing L-ornithine and urea. In this study, the physicochemical properties of Oryctes rhinoceros Larva arginase were investigated for biochemical comparison with its well-studied terrestrial mammalian. Oryctes rhinoceros larva arginase was isolated and purified to homogeneity. The purification procedure involved ion-exchange chromatography on DEAE-cellulose and affinity chromatography on reactive Blue 2-agarose. The pure enzyme had a specific activity of 38.7 U/mg, a purification fold of 63.4, and a percentage yield of 16.5%. O. rhinoceros gut arginase had a native and subunit molecular weight of 82 and 45 kDa, respectively and the Km and Vmax were 11.25 mM and 13.055 μmmol/min/mL, respectively. The activity was optimum at 60 °C m max (pH 8). The enzyme retained more than 60% of its activity at 50 °C for 60 min. The inhibition study on the enzyme showed that cations salts (CaCl2 , BaCl2 , HgCl2 , and SnCl2 ) enhanced the enzyme activity at 1 mM concentration except for SnCl2 . EDTA, a chelating compound, strongly inhibited the activity of the enzyme. The 2 effect of different amino acids on activity showed that L-valine, L-serine, L- aspartic acid, and L-glutamic acid had a moderate inhibitory (60%, 63%, 65.4%, 69.1%, respectively) effect on the enzyme activity. The study concluded that there were similarities between O. rhinoceros larva arginase and those of other ureotelic animals in terms of kinetics and physicochemical properties.

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Section: Discussionmentioning

confidence: 99%

Biochemical characterization of a purified arginase from the gut of Oryctes rhinoceros larvae

Famakinwa¹,

Itakorode²,

Adedeji³

et al. 2023

ijs

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“…Arginase, an enzyme known to catalyse the conversion of arginine to urea becomes more effective in aquatic organisms, especially fresh water fishes when their environment becomes polluted and made more alkaline (Campbell and Anderson, 1991;Mommsen and Walsh, 1992;Wood, 1993). During the rainy season, allochotonous materials flushed into the reservoir and affected its status (Eisler, 1991;Okonji et al, 2010Okonji et al, , 2011. Saha and Ratha (2007) had also reported Heteropneustes fossilis and C. batrachus to be hardy and capable of living in derelict water bodies and tolerating temporary water deprivation.…”

Section: Discussionmentioning

confidence: 99%

“…Despite the generalization above, the urea pathway has been documented not only in mammals and amphibians but in many other organisms such as birds, invertebrates, insects, plants, yeast, fungi and microorganisms. Environmental conditions have also been reported to be the common stimulus for urea synthesis in some fishes (Campbell and Anderson, 1991;Okonji et al, 2011). Anthropogenic impacts on fish populations in Osinmo and other reservoirs in the Southwestern Nigeria include not only water pollution, but also the extensive fishery, as well as habitat destruction by dam building and river modifications (Lenhardt et al, 2004;Atobatele, 2008;Komolafe and Arawomo, 2008;Okonji et al, 2011).…”

Section: Introductionmentioning

confidence: 99%

“…Environmental conditions have also been reported to be the common stimulus for urea synthesis in some fishes (Campbell and Anderson, 1991;Okonji et al, 2011). Anthropogenic impacts on fish populations in Osinmo and other reservoirs in the Southwestern Nigeria include not only water pollution, but also the extensive fishery, as well as habitat destruction by dam building and river modifications (Lenhardt et al, 2004;Atobatele, 2008;Komolafe and Arawomo, 2008;Okonji et al, 2011). In addition, temperature and water levels are both crucial factors affecting enzyme activities in aquatic environment.…”

Section: Introductionmentioning

confidence: 99%

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Effects of seasonal change in Osinmo reservoir on arginase and rhodanese activities in Clarias gariepinus Burchell and Heterotis niloticus Cuvier

Okonji¹,

Komolafe²,

Popoola³

et al. 2013

Afr. J. Agric. Res.

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This work reports the seasonal change and variation in the physico-chemical properties of the water inOsinmo reservoir in Southwestern Nigeria and the effects on tissue distribution of the metabolic enzymes, arginase and rhodanese are the two fish species (Clarias gariepinus and Heterotis niloticus) collected from the reservoir. This study was carried out to correlate the activities of the enzymes with metabolic status of the fishes and physico-chemical properties of the water. The enzyme activities varied significantly in the different tissues of the C. gariepinus. The liver showed the highest mean value of activity and the intestine had the least mean value. In the H. niloticus, they showed the highest mean value of activity while the bile showed the lowest mean value. The activities of the two enzymes in the water reservoir were determined at regular intervals over a period of ten months in 2011, spanning both dry and rainy seasons. The activities of the enzymes varied significantly through the two seasons. Arginase was at its peak in June while rhodanese was at its peak in September. The distribution of urea in the reservoir varied significantly in the period studied; the highest mean value was in July while the lowest was in February.

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The Distribution of the Enzyme Arginase in the Tissues of Selected Cichlidae Species: <i>Tilapia zillii, Sarotherodon galilaeus</i> and <i>Oreochromis niloticus</i>

Cited by 2 publications

References 26 publications

Biochemical characterization of a purified arginase from the gut of Oryctes rhinoceros larvae

Biochemical characterization of a purified arginase from the gut of Oryctes rhinoceros larvae

Effects of seasonal change in Osinmo reservoir on arginase and rhodanese activities in Clarias gariepinus Burchell and Heterotis niloticus Cuvier

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