Characterization of arginase from the liver of mango tilapia (sarotherodongalilaeus)

• <p> </p><div><p><strong>HAPTER ONE: INTRODUCTION AND LITERATURE REVIEW</strong></p><p>1.o &nbsp; &nbsp; &nbsp; Introduction</p><p>
• 1.2&nbsp; &nbsp; &nbsp; Classification</p><p>
• 1.3&nbsp; &nbsp; &nbsp; Distribution and occurrence</p><p>
• 1.4&nbsp; &nbsp; &nbsp; Literature review</p><p>1.
• 4.1&nbsp; Arginase</p><p>1.
• 4.2&nbsp; Arginase isoenzymes</p><p>
• 1.5&nbsp; &nbsp; &nbsp; Structural properties</p><p>1.
• 5.1&nbsp; Molecular properties</p><p>1.
• 5.2&nbsp; Amino acid composition</p><p>
• 1.6&nbsp; &nbsp; &nbsp; Physicochemical properties</p><p>1.
• 6.1&nbsp; Kinetic properties</p><p>1.
• 6.2&nbsp; Effect of p H</p><p>1.
• 6.3&nbsp; Effect of temperature</p><p>1.
• 6.4&nbsp; Effect of metal ions</p><p>
• 1.7&nbsp; &nbsp; &nbsp; Mechanism of action</p><p>
• 1.8&nbsp; &nbsp; &nbsp; Arginase deficiency</p><p>
• 1.9&nbsp; &nbsp; &nbsp; Biological and physiological importance of arginase</p><p>
• 1.10&nbsp; &nbsp; Study sample</p><p>1.
• 10.1Taxonomy</p><p>1.
• 10.2Morphology</p><p>1.
• 10.3Distribution</p><p>1.
• 10.4Ecology</p><p>1.
• 10.5Biology</p><p>1.
• 10.6Feeding habits</p><p>1.
• 10.7Reproduction and parental care</p><p>1.
• 10.8Economic importance</p><p>
• 1.11&nbsp; &nbsp; Liver</p><p>
• 1.12&nbsp; &nbsp; Objectives</p><p>

Chapter TWO

LITERATURE REVIEW

• MATERIALS AND METHODS</p><p>
• 2.1&nbsp; &nbsp; &nbsp; Materials</p><p>2.
• 1.1&nbsp; Chemicals and reagents</p><p>2.
• 1.2&nbsp; Equipments</p><p>
• 2.2&nbsp; &nbsp; &nbsp; Methods</p><p>2.
• 2.1&nbsp; Enzyme isolation</p><p>2.
• 2.2&nbsp; Preparation of buffer and reagents</p><p>2.2.
• 2.10.33M Arginine</p><p>2.2.
• 2.2Bradford reagent</p><p>2.2.
• 2.3Erlich reagent</p><p>2.2.
• 2.4Homogenization buffer (0.1M Phosphate buffer)</p><p>2.2.
• 2.50.1M Citrate buffer, p H 3.0</p><p>2.2.
• 2.60.1M Trizma HCl buffer, p H 6.0</p><p>2.2.
• 2.70.1M Trizma HCl buffer, p H 7.0</p><p>2.2.
• 2.80.1M Trizma HCl buffer, p H 9.0</p><p>2.2.
• 2.9Arginase assay</p><p>2.2.
• 2.10Protein assay</p><p>2.2.
• 2.11Determination of kinetic parameters</p><p>2.2.
• 2.12Effect of p H on enzyme activity</p><p>2.2.
• 2.13Effect of temperature on enzyme activity</p><p>2.2.
• 2.14Effect of amino acids on enzyme activity</p><p>2.2.
• 2.15Effect of chelating compounds on arginase activity</p><p>2.2.
• 2.16Effect of metal ions on arginase activity</p><p>

Chapter THREE

RESEARCH METHODOLOGY

• RESULTS</p><p>
• 3.1Effect of temperature</p><p>
• 3.2Effect of pH</p><p>
• 3.3Kinetic study</p><p>
• 3.4Inhibition study</p><p>3.
• 4.1Effect of chelating compounds</p><p>3.
• 4.2Effect of divalent metals</p><p>3.
• 4.3Effect of amino acids</p><p>

Chapter FOUR

DATA PRESENTATION AND ANALYSIS

• DISCUSSION, CONCLUSION AND RECOMMENDATION</p><p>
• 4.1&nbsp; &nbsp; &nbsp; Discussion</p><p>
• 4.2&nbsp; &nbsp; &nbsp; Conclusion</p><p>
• 4.3&nbsp; &nbsp; &nbsp; Recommendation</p><p>References</p><p>LIST OF TABLES</p><p>Table
• 3.1&nbsp; Effect of temperature on arginase activity</p><p>Table
• 3.2&nbsp; Effect of pH on arginase activity</p><p>Table
• 3.3&nbsp; Kinetic study</p><p>Table
• 3.4&nbsp; Effect of chelating compounds</p><p>Table
• 3.5&nbsp; Effect of divalent metals</p><p>Table
• 3.6&nbsp; Effect of amino acids</p><p>LIST OF FIGURES</p><p>Figure
• 1.1&nbsp; &nbsp; &nbsp; External structure of mango tilapia</p><p>Figure
• 3.1&nbsp; &nbsp; &nbsp; Graph of temperature against activity</p><p>Figure
• 3.2&nbsp; &nbsp; &nbsp; Graph of pH against activity</p><p>Figure
• 3.3&nbsp; &nbsp; &nbsp; Determination of Km and Vmax</p><p></p></div><h3></h3><br> <br><p></p>