請用此 Handle URI 來引用此文件: http://hdl.handle.net/11455/35794
標題: I:人類 6-磷酸葡萄糖異構酵素與鳥苷三磷酸結合及其遺傳性突變之結構與功能關聯性研究 II: 竹嵌紋病毒戴帽酵素中保留性組胺酸於形成[酵素-m7GMP]中間產物時之功能分析
I: Structure-function relationship of human phosphoglucose isomerase – A study bases on inherited mutations and GTP-binding II: Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the covalent [Enzyme-m7GMP] intermediate formation
作者: 林華洋
Lin, Hua-Yang
關鍵字: 人類 6-磷酸葡萄糖異構酵素
phosphoglucose isomerase
鳥苷三磷酸
竹嵌紋病毒
戴帽酵素
非球形紅血球溶血性貧血
熱卡儀
HNSHA
GTP
BaMV, bamboo mosaic virus
capping enzyme
hydroxylamine
ITC
DSC
出版社: 生物科技學研究所
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摘要: 本論文分為兩個部份,第一個部份為“人類 6-磷酸葡萄糖異構酵素與鳥苷三磷酸結合及其遺傳性突變點之結構與功能關聯性研究”,包含兩個章節,第一章為“人類6-磷酸葡萄糖異構酵素非球形紅血球溶血性貧血相關遺傳性突變對酵素活性與穩定性影響之探討”,主要是探討已知之非球形紅血球溶血性貧血相關遺傳性突變對人類 6-磷酸葡萄糖異構酵素在酵素動力學參數,和蛋白質熱穩定性之影響,以增進對人類 6-磷酸葡萄糖異構酵素結構與功能關係的瞭解。 第二章為“人類6-磷酸葡萄糖異構酵素與鳥苷三磷酸結合之特性探討”。人類6-磷酸葡萄糖異構酵素與鳥苷三磷酸有ㄧ未被報導過的結合,此章節將探討此結合的生化和生物特性。第二個部份為“竹嵌紋病毒戴帽酵素中保留性組胺酸於形成[酵素-m7GMP]中間產物時之功能分析”。此部份將利用化學性截切和突變後的化學特性轉變,探討在形成[酵素-m7GMP]中間產物時組胺酸H66 和保留性組胺酸H68 的所扮演的角色。
The part I in this dissertation is “Structure-function relationship of human phosphoglucose isomerase − A study bases on inherited mutations and GTP-binding”. This part contains two chapters. Chapter I entitled “Effects of inherited mutations on catalytic activity and structural stability of human phosphoglucose isomerase expressed in Escherichia coli” demonstrates the effects of the inherited mutations associated with nonspherocytic hemolytic anemia on the protein properties including kinetic parameter and protein stability. Chapter II entitled “Characterization of the novel binding of GTP to human phosphoglucose isomerase/autocrine motility factor” explicates a novel binding between human phosphoglucose isomerase and GTP. The biochemical and biological characterization of this binding is described in this chapter. The part II is “Functional analysis of the conserved histidine residue of Bamboo mosaic virus capping enzyme in the activity for the covalent [Enzyme-m7GMP] intermediate formation”. In this part, the amino acid residue that covalently bond to m7GMP was identified using hydroxylamine digestion mapping and mutagenesis assay. The roles of the histidine residue, H66, and the conserved histidine residue, H68, on the formation of [Enzyme-m7GMP] intermediate were also investigated.
URI: http://hdl.handle.net/11455/35794
其他識別: U0005-0907201212162300
文章連結: http://www.airitilibrary.com/Publication/alDetailedMesh1?DocID=U0005-0907201212162300
顯示於類別:生物科技學研究所

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