<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>1.10.1 Taxonomy</p><p>1.10.2 Morphology</p><p>1.10.3 Distribution</p><p>1.10.4 Ecology</p><p>1.10.5 Biology</p><p>1.10.6 Feeding habits</p><p>1.10.7 Reproduction and parental care</p><p>1.10.8 Economic importance</p><p>1.11 &nbsp; &nbsp; Liver</p><p>1.12 &nbsp; &nbsp; Objectives</p><p>

Chapter TWO

: 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>2.2.2.1 0.33M Arginine</p><p>2.2.2.2 Bradford reagent</p><p>2.2.2.3 Erlich reagent</p><p>2.2.2.4 Homogenization buffer (0.1M Phosphate buffer)</p><p>2.2.2.5 0.1M Citrate buffer, p H 3.0</p><p>2.2.2.6 0.1M Trizma HCl buffer, p H 6.0</p><p>2.2.2.7 0.1M Trizma HCl buffer, p H 7.0</p><p>2.2.2.8 0.1M Trizma HCl buffer, p H 9.0</p><p>2.2.2.9 Arginase assay</p><p>2.2.2.10 Protein assay</p><p>2.2.2.11 Determination of kinetic parameters</p><p>2.2.2.12 Effect of p H on enzyme activity</p><p>2.2.2.13 Effect of temperature on enzyme activity</p><p>2.2.2.14 Effect of amino acids on enzyme activity</p><p>2.2.2.15 Effect of chelating compounds on arginase activity</p><p>2.2.2.16 Effect of metal ions on arginase activity</p><p>

Chapter THREE

: RESULTS</p><p>3.1 Effect of temperature</p><p>3.2 Effect of pH</p><p>3.3 Kinetic study</p><p>3.4 Inhibition study</p><p>3.4.1 Effect of chelating compounds</p><p>3.4.2 Effect of divalent metals</p><p>3.4.3 Effect of amino acids</p><p>

Chapter FOUR

: 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>