Return to search

A biochemical study of defense proteins: hemagglutinin, hemolysin and antifungal protein.

Leung, Ho Wai. / Thesis (M.Phil.)--Chinese University of Hong Kong, 2007. / Includes bibliographical references (leaves 136-146). / Abstracts in English and Chinese. / THESIS COMMITTEE --- p.II / ACKNOWLEDGEMENT --- p.III / ABSTRACT --- p.IV / CHINESE ABSTRACT --- p.VI / TABLE OF CONTENT --- p.VII / OVERVIEW OF THIS PROJECT --- p.1 / Chapter SECTION 1: --- Purification and Characterization of hemagglutinins from French bean and mottled kidney bean / Chapter Chapter 1 --- INTRODUCTION / Chapter 1.1 --- General Introduction --- p.2 / Chapter 1.2 --- Physiological functions of plant lectins --- p.6 / Chapter 1.3 --- Physiological functions of animal lectins --- p.9 / Chapter 1.4 --- Biological functions of lectins --- p.12 / Chapter 1.5 --- Clinical and research applications of lectins --- p.16 / Chapter 1.6 --- Legume lectins --- p.17 / Chapter 1.7 --- Isolation and purification of lectins --- p.19 / Chapter 1.8 --- Objectives of the present study --- p.21 / Chapter Chapter 2 --- MATERIALS AND METHODS / Chapter 2.1 --- Chemicals --- p.22 / Chapter 2.2 --- Assay of hemagglutinating activity --- p.24 / Chapter 2.3 --- Purification protocol --- p.26 / Chapter 2.4 --- Assay of saccharide inhibition of hemagglutination --- p.28 / Chapter 2.5 --- Assay of pH stability --- p.28 / Chapter 2.6 --- Molecular mass determination and N-terminal sequence determination --- p.28 / Chapter 2.7 --- Assay of mitogenic activity --- p.29 / Chapter 2.8 --- Assay of antiproliferative activity --- p.30 / Chapter 2.9 --- Assay for antifungal activity --- p.30 / Chapter 2.10 --- Assay of HIV-1 reverse transcriptase inhibitory activity --- p.31 / Chapter 2.11 --- Assay of stability towards trypsin and chymotrypsin --- p.31 / Chapter 2.12 --- Assay of nitric oxide production --- p.32 / Chapter 2.13 --- Assay ofHIV-1 integrase --- p.32 / Chapter Chapter 3 --- EXPERIMENTAL RESULTS / Chapter 3.1 --- Purification scheme --- p.35 / Chapter 3.2 --- Size determination and N-terminal sequencing --- p.36 / Chapter 3.3 --- Temperature stability assay --- p.37 / Chapter 3.4 --- pH stability assay --- p.37 / Chapter 3.5 --- Saccharides inhibition of hemagglutination --- p.37 / Chapter 3.6 --- Stability towards Trypsin and Chymotrypsin --- p.38 / Chapter 3.7 --- Anti-proliferative activity --- p.38 / Chapter 3.8 --- HTV-1 reverse transcriptase inhibition --- p.39 / Chapter 3.9 --- Mitogenic activity --- p.39 / Chapter 3.10 --- Nitric oxide production --- p.39 / Chapter 3.11 --- HIV-1 integrase --- p.39 / Chapter 3.12 --- Defensin --- p.40 / Chapter Chapter 4 --- DISCUSSION / Chapter 4.1 --- Purification scheme --- p.68 / Chapter 4.2 --- Sequence comparison --- p.69 / Chapter 4.3 --- Physical Stability of the hemagglutinins --- p.70 / Chapter 4.4 --- Protease Stability --- p.71 / Chapter 4.5 --- Sugar Specificity Assay --- p.72 / Chapter 4.6 --- Anti-proliferative Aactivity toward Cancer Cells --- p.73 / Chapter 4.7 --- HTV-1 reverse trancriptase and H̐ơþV integrase inhibition --- p.74 / Chapter 4.8 --- Mitogenic activity --- p.75 / Chapter 4.9 --- Antifungal protein --- p.76 / Chapter Chapter 5 --- CONCLUSION --- p.78 / Chapter SECTION 2: --- Purification and Characterization of flammulolysin from mushroom Flαmmulinα velutipes / Chapter Chapter 1 --- INTRODUCTION / Chapter 1.1 --- General Introduction --- p.79 / Chapter 1.2 --- Mechanisms of hemolysis --- p.80 / Chapter 1.3 --- Biological role of hemolysins --- p.80 / Chapter 1.4 --- Mushroom hemolysin --- p.82 / Chapter 1.5 --- Applications of hemolysins --- p.83 / Chapter 1.6 --- Objectives of the present study --- p.83 / Chapter Chapter 2 --- MATERIALS AND METHODS --- p.84 / Chapter Chapter 3 --- EXPERIMENTAL RESULTS / Chapter 3.1 --- Purification and sequence determination --- p.90 / Chapter 3.2 --- Effect of sugars and salts on hemolysin --- p.90 / Chapter 3.3 --- Effect of Temperature and pH on hemolysin --- p.91 / Chapter 3.4 --- Effect of Proteases on hemolysin --- p.91 / Chapter 3.5 --- Effect of osmotic protection on hemolysin --- p.91 / Chapter 3.6 --- Effect of hemolysin on tumor cells --- p.91 / Chapter 3.7 --- Effect of hemolysin on spleen cells --- p.92 / Chapter 3.8 --- Effect of hemolysin on bacterial growth --- p.92 / Chapter 3.9 --- Effect of hemolysin on fungal growth --- p.92 / Chapter Chapter 4 --- DISCUSSION / Chapter 4.1 --- Purification and sequence comparison of hemolysin --- p.103 / Chapter 4.2 --- Sugar and Salts inhibition --- p.104 / Chapter 4.3 --- Temperature stability --- p.105 / Chapter 4.4 --- pH stability --- p.106 / Chapter 4.5 --- Protease stability --- p.106 / Chapter 4.6 --- Osmotic Protection --- p.106 / Chapter 4.7 --- Anti-tumour activity of the hemolysin --- p.107 / Chapter 4.8 --- Anti-fungal activity --- p.108 / Chapter Chapter 5 --- CONCLUSION --- p.109 / Chapter SECTION 3: --- Purification and Characterization of antifungal peptide from buckwheat seeds Fagopyrum esculentum / Chapter Chapter 1 --- INTRODUCTION / Chapter 1.1 --- Plant antiftmgal proteins --- p.110 / Chapter 1.2 --- Classification of antifungal proteins --- p.110 / Chapter 1.3 --- Distribution of antifungal proteins in plants --- p.111 / Chapter 1.4 --- Mechanisms of antifungal activity --- p.111 / Chapter 1.5 --- Future Perspectives of Antifungal proteins --- p.112 / Chapter 1.6 --- Antifungal peptide from Buckwheat --- p.112 / Chapter 1 .7 --- Objectives of the present study --- p.113 / Chapter Chapter 2 --- MATERIALS AND METHODS --- p.114 / Chapter Chapter 3 --- EXPERIMENTAL RESULTS / Chapter 3.1 --- Purification and sequence determination --- p.118 / Chapter 3.2 --- Effect on anti-fungal activity --- p.118 / Chapter 3.3 --- Effect of temperature and pH on antifungal activity --- p.118 / Chapter 3.4 --- Effect of the antifungal peptide on tumor cells --- p.119 / Chapter 3.5 --- Effect of antifungal peptide on HIV-1 Reverse transcriptase Activity --- p.119 / Chapter 3.6 --- Effect of antifungal peptide on spleen cells and NO Production --- p.119 / Chapter Chapter 4 --- DISCUSSION / Chapter 4.1 --- Purification scheme and N-terminal sequence --- p.130 / Chapter 4.2 --- Antifungal Activity --- p.131 / Chapter 4.3 --- Physical stability --- p.131 / Chapter 4.4 --- Anti-proliferative activity toward cancer cells --- p.131 / Chapter 4.5 --- HTV-1 Reverse Transcriptase Inhibitory activity --- p.132 / Chapter 4.6 --- Mitogenic activity and nitric oxide production --- p.132 / Chapter Chapter 5 --- CONCLUSION --- p.133 / OVERALL CONCLUSION --- p.134 / REFERENCES --- p.136

Identiferoai:union.ndltd.org:cuhk.edu.hk/oai:cuhk-dr:cuhk_326033
Date January 2007
ContributorsLeung, Ho Wai., Chinese University of Hong Kong Graduate School. Division of Biochemistry.
Source SetsThe Chinese University of Hong Kong
LanguageEnglish, Chinese
Detected LanguageEnglish
TypeText, bibliography
Formatprint, x, 146 leaves : ill. ; 30 cm.
RightsUse of this resource is governed by the terms and conditions of the Creative Commons “Attribution-NonCommercial-NoDerivatives 4.0 International” License (http://creativecommons.org/licenses/by-nc-nd/4.0/)

Page generated in 0.0026 seconds