ABSTRACT
The research is aimed at investigating the effect of sodium citrate and reduced glutathione (GSH) on arginase from human fibriod tissue.
The research shows that arginase enzyme which was partially purified was found to have a specific interaction with its substrate.
The study shows that varying the substrate concentration at constant volume of Sodium citrate and Reduced glutathione (GSH) resulted into an Un-competitive inhibition and Competitive inhibition of enzymes respectively.
The results obtained from this study shows that the inhibition nature of arginase by different inhibitors of enzymes gives a promising approach to abnormal arginase activities in cell proliferation of uterine muscle which leads to fibroid.
TABLE OF CONTENTS
Abstract
CHAPTER ONE
1.0 Introduction and Literature Review
1.1 Fibroid
1.1.1 Location and classification of fibroid
1.1.2 Pathogenesis and Pathophysiology
1.1.2.1 Pathogenesis
1.1.2.2 Pathophysiology
1.1.3 Signs, Symptoms and Causes of fibroid
1.2 Arginase
1.2.1 Role of arginase in human body
1.2.2 Aginase activities in Benign tumour
1.2.3 Arginase II expression in benign and malignant prostate tissue
1.3 Glutathione (GSH)
1.3.1 Role of glutathione as an antioxidant
1.3.2 Glutathione response to exercise
1.4 Sodium citrate
1.5 Aims and objectives
CHAPTER TWO
2.0 Materials and Methods
2.1 Materials
2.1.1 Apparatus
2.2 Methods
2.2.1 Preparation of buffers and reagents
2.3 Biochemical test
2.3.1 Arginase assay
2.3.2 Protein standard curve
2.3.3 Effect of Glutathione (GSH)
CHAPTER THREE
3.0 Results
CHAPTER FOUR
4.0 Discussion, Conclusion and Recommendation
4.1 Discussion
4.2 Conclusion
4.3 Recommendations
References
LIST OF FIGURES
Figure 1 – Uterine Fibroid
Figure 2 – Hydrolysis of L-arginine
Figure 3 – Structure of arginase and the active site
Figure 4 – Showing the effect of sodium citrate on arginase from human fibroid tissue
Figure 5 – Showing the effect of Glutathione (GSH) on arginase from human fibroid tissue.
