PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT

PARTIAL PURIFICATION AND EFFECT OF TEMPERATURE AND HEAT STABILITY STUDIES ON RHODANESE FROM THE LIVER OF A LOCAL GOAT
 
ABSTRACT
The research is aimed at investigating the effect of temperature and heat stability of Rhodanese from the Liver of a local goat.  This research shows the existence of rhodanese from a local goat liver homogenate. It was observed that the enzyme was partially purified by ammonium sulphate precipitation and dialysis. The specific activity of enzyme after partial purification using ammonium sulphate precipitation and dialysis was 4.39 U/mg. The effect of temperatures between 30 and 80◦C on the rhodanese activity showed that optimum temperature for the enzyme was at 60◦C. It was found that the enzyme (rhodanese) from a local goat liver was stable at 60◦C, but was unstable at temperatures ≥ 70◦C.
 
TABLE OF CONTENTS
CHAPTER ONE
1.0     Introduction
1.1     Aim of research
CHAPTER TWO
2.0     Literature Review
2.1     Physiochemical features of rhodanese
2.1.1  Mechanism of action
2.1.2  Assay methods for rhodanese
2.1.3  Mechanism of rhodanese catalysis
2.1.4  Structure
2.1.5  Amino acid composition
2.1.6  Active sites
2.2     Goat
2.3     Liver
2.3.1  Synthesis
2.3.2  Liver disease
2.3.3  Fetal blood supply
CHAPTER THREE
3.0     Materials and Methods
3.1     Materials used
3.2     Reagents used
3.3     Preparation of buffer and reagents used
3.4     Collection of sample
3.5     Preparation of tissue extract
3.6     Enzyme assay
3.7     Protein determination
3.8     Effect of temperature on rhodanese
3.9     Purification of rhodanese from crude extract
3.10   Determination of protein concentration and enzyme activities
CHAPTER FOUR
4.0     Results
CHAPTER FIVE
5.0     Discussion, Conclusion and Recommendation
5.1     Discussion
5.2     Conclusion
5.3     Recommendations
References.