STUDY ON THE DESTABILIZATION OF LYSOZYME AND THE CHAPERONE-LIKE ACTIVITY OF ALPHA CRYSTALLIN FROM SOKOTO RED GOAT EYE LENS

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ABSTRACT


Destabilization of Lysozyme and chaperone like action of alpha crystallin isolated from goat’s eye lens was investigated at various temperature ranges in phosphate buffer (pH 7.1) solution and dithiothretol (DTT). This was monitored spectrophotometrically at 260nm. The heat and DTT-induced destabilization of lysozyme was prevented by alpha crystallin in a concentration dependent manner. Alpha crystallin like other chaperones, fulfils its chaperone like action in preventing aggregation of denatured proteins by the formation of complexes.


TABLE OF CONTENTS

TITLE PAGE
TABLE OF CONTENTS
LIST OF TABLES
LIST OF FIGURES
ABSTRACT

CHAPTER ONE
INTRODUCTION AND LITERATURE REVIEW
1.0       INTRODUCTION
1.1.1 PROTEIN FOLDING
1.1.2    PROTEIN DENATURATION
1.1.3 CRYSTALLINS
1.1.4 JUSTIFICATION
1.1.5 AIM AND OBJECTIVES
1.2       LITERATURE REVIEW
1.2.1 α-CRYSTALLINS: PROPERTIES, OCCURANCE AND FUNCTIONS
1.2.2    FUNCTIONS OF ALPHA CRYSTALLIN AND ITS RELATION SHSPS
1.2.3 GENE STRUCTURE, EXPRESSION AND REGULATION
1.2.4 QUATERNARY STRUCTURE MODELS OF CRYSTALLIN
1.2.5    IN VITRO MODIFICATIONS OF ALPHA CRYSTALLIN
1.2.6    FUNCTION OF CRYSTALLIN
1.2.7    LYSOZYME
1.2.8    DITHIOTHRETOL
1.2.9    LENS

CHAPTER TWO
2.0 MATERIALS AND METHODS
2.1 MATERIALS
2.1.1 REAGENTS AND EQUIPMENT
2.1.2 APPARATUS USED FOR CHROMATOGRAPHY
2.2 METHODS
2.2.1 PREPARATION OF ALPHA CRYSTALLIN
2.2.2 DETERMINATION OF ALPHA CRYSTALLIN
2.2.3 ESTIMATION OF PROTEIN BY FOLIN-CIOCALTEU [LOWRY]  METHOD
2.2.4 PURIFICATION OF CRYSTALLIN USING GEL CHROMATOGRAPHY
2.2.5 TEMPERATURE DESTABILIZATION OF OXIDIZED LYSOZYME AND CHAPERONE EFFECT OF ALPHA CRYSTALLIN

CHAPTER THREE
3.0 RESULTS, DISCUSSION AND CONCLUSION
3.1 RESULTS
3.2 DISCUSSION
3.3 CONCLUSION
REFERENCES
APPENDICES


CHAPTER ONE

1.0 INTRODUCTION AND LITERATURE REVIEW

1.1 INTRODUCTION


Proteins are the workhorses of the living cell. Although proteins may differ in sequence, shape and function, but have in common, the same stereo configuration (i.e. they all have to fold into specific three-dimensional structures) which are mandatory for proper function (Bruce et al., 2002). Protein structures however are not rigid, but have a dynamic life style, which may involve unfolding and refolding, complex association and dissociation (Anfisen, 1972). Stress and also many physiological events require proteins to surrender their structure or to regain it at a later stage. A very large number of distinct conformations exist for the polypeptide chain of which a protein spends most of its time in the native conformation, which spans only an extremely small fraction of the entire configuration space. Thus, the amino acid sequence of proteins must satisfy two requirements: one, thermodynamics and the other kinetic. The thermodynamics requirement is that the sequence must have a unique folded conformation, which is stable under physiological conditions.


Most proteins can be denatured by heat, which has complex effect on the weak interactions in proteins (Vandenberg et al., 2000). If the existing temperature is increased slowly, a protein conformation generally remains intact until an abrupt loss of structure and function occurs over a narrow temperature range (Nelson and Cox, 2008). The spatial arrangement of atoms in a protein is called its conformation (Deechongkit et al., 2004). The possible conformations of a protein include any structural state it can achieve....


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