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研究生:柯泰裕
研究生(外文):Tai -Yu Kuo
論文名稱:人類粒線體型重組醛脫氫次單元組成與分子活性表現之機制
論文名稱(外文):Subunit Composition and Expression of Molecular Activity of Recombinant Human Mitochondrial Aldehyde Dehydrogenase
指導教授:尹士俊
指導教授(外文):Shih-Jiun Yin
學位類別:碩士
校院名稱:國防醫學院
系所名稱:生物化學研究所
學門:生命科學學門
學類:生物化學學類
論文種類:學術論文
論文出版年:1999
畢業學年度:87
語文別:中文
論文頁數:62
中文關鍵詞:醛脫氫醇脫氫
外文關鍵詞:aldehyde dehydrogenasealcohol dehydrogenase
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哺乳動物肝臟中乙醇代謝產物乙醛的氧化主要是由細胞液型ALDH1及粒線體型ALDH2負責。將含人類ALDH1、ALDH2E、ALDH2K及ALDH2E/K的cDNA之載體,在大腸桿菌表現,經DEAE Sepharose與p-HAP Sepharose層析可達均質,次單元分子量均為55 kD。對乙醛的催化效率ALDH2E > ALDH2E/K > ALDH1 > ALDH2K。等電焦集電泳顯示ALDH2E/K的四次單元分子混合物中,E4:E3K:E2K2:EK3:K4的蛋白質含量測定比值接近 1:4:6:4:1,且E4:E3K:E2K2:EK3:K4的活性染色強度比值接近1:2:1:0:0。這項結果支持下述論點:(1)ALDH2的E及K次單元可隨機組合成四次單元分子,(2)四次單元分子以雙次單元為其組合單位,(3)E2K2有EE-KK與EK-EK兩種組合方式存在,(4)雙四次單元分子中僅一半的活性中心具催化活性,(5)K次單元對雙次單元的失活為顯性。上述對ALDH2E/K混合物的分子組成及活性表現模式與不同ALDH2對偶基因型手術肝檢體的蛋白質含量和活性的測定結果一致。

Cytosolic aldehyde dehydrogenase-1(ALDH1)and mitochondrial ALDH2 are the principal enzymes responsible for oxidation of acetaldehyde, a major metabolite of ethanol, in mammalian livers. Recombinant human ALDH1, ALDH2E, ALDH2K, and ALDH2E/K were isolated from E. coli transformed with plasmids of the expression vectors harboring cDNAs of the respective enzymes, and purified via DEAE—Sepharose and p-hydroxyacetophenone—Sepharose chromatographies to apparent homogeneity. The molecular weights of the ALDH1 and ALDH2 forms were determined to be ~55 kD. Catalytic efficiencies for oxidation of acetaldehyde were found in the following order: ALDH2E > ALDH2E/K > ALDH1 > ALDH2K. Using polyacrylamide isoelectric focusing, protein content ratios for bands of the tetrameric ALDH2E/K mixture were quantitated to be E4 : E3K : E2K2 : EK3 : K4 = 1 : 4 : 6 : 4 : 1 as well as ratios for the activity staining intensities, E4 : E3K : E2K2 : EK3 : K4 = 1 : 2 : 1 : 0 : 0. These results strongly support that (a) the E and K subunits can randomly combine to form homo- and heterotetrameric ALDH2 molecules; (b) dimers act as the forming unit for the tetrameric molecules; (c) both the EE-KK and EK-EK exist in the E2K2 molecules; (d) ALDH2 exhibits half-of-the-sites activity; (e) the K subunits function dominantly over loss of the enzyme activity in the dimer units. The proposed molecular model for the subunit composition and enzymatic activity of the recombonant tetrameric ALDH2E/K mixture appears to be in agreement with recent findings of the protein contents and activities of mitochondrial ALDH2 expressed in the human livers with homo- and heterozygous ALDH2 genotypes.

目錄‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅰ
附表目錄‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅲ
插圖目錄‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅳ
縮寫表‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅴ
中文摘要‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅵ
英文摘要‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧Ⅶ
緒言‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧1
材料與方法‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧7
壹、實驗材料‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧7
一、化學藥品‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧7
二、主要儀器‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧8
三、其他用品‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧8
四、人類重組ALDH1、ALDH2E、ALDH2K及ALDH2E/K cDNA之表現載體‧‧8
五、人類手術肝黏膜檢體之收集‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧9
貳、實驗方法‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧9
一、 對位羥基苯乙酮(p-hydroxyacetophenone, p-HAP)親力樹脂之合
成‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 9
二、醛脫氫活性之測定‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧9
三、重組ALDH載體在大腸桿菌宿主表現菌落之篩選‧‧‧‧‧‧‧‧ 10
四、人類重組ALDH之純化‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 10
五、肝組織上清液之製備‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 11
六、蛋白質電泳‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 11
七、免疫轉漬分析‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 12
八、純度之判斷標準‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 13
九、蛋白質濃度之測定‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 13
十、人類重組ALDH2E、ALDH2K與ALDH2E/K比活性之測定‧‧‧‧‧‧ 13
十一、動力學測定及常數分析‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 14
十二、聚丙烯醯膠等電焦集電泳(IEF)染色帶之定量‧‧‧‧‧‧‧14
實驗結果‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 15
壹、重組ALDH載體在大腸桿菌宿主表現菌落之篩選‧‧‧‧‧‧‧‧ 15
貳、人類重組ALDH之純化‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 16
參、人類重組ALDH1、ALDH2E、ALDH2K及ALDH2E/K之動力學特性‧‧‧18
肆、人類重組ALDH1、ALDH2E、ALDH2K及ALDH2E/K的比活性之比較‧‧18
伍、人類ALDH2以次單元作為組合單位,其四次單元分子之理論
隨機組合方式‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 19
陸、人類重組ALDH2E/K異四次單元分子蛋白質組合之分佈‧‧‧‧‧ 19
柒、人類重組ALDH2E/K異四次單元分子活性組合之分佈‧‧‧‧‧ 19
討論‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 21
壹、人類重組ALDH1、ALDH2E、ALDH2K與ALDH2E/K之蛋白質
表現及純化‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 21
貳、人類重組ALDH1、ALDH2E、ALDH2K與ALDH2E/K之動力學特性‧‧‧22
參、人類ALDH2E/K異四次單元分子混合物之探討‧‧‧‧‧‧‧‧‧ 23
結論‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 26
參考文獻‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧‧ 27

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