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    Please use this identifier to cite or link to this item: http://ir.lib.ncu.edu.tw/handle/987654321/6273


    Title: 亞砷酸鈉與Galectin-1蛋白交互作用之研究;The study of interaction of arsenite and galectin-1
    Authors: 黃琦斐;Chi-Fei Huang
    Contributors: 生命科學研究所
    Keywords: 亞砷酸鈉;固相結合試驗;solid phase binding assay;ITC;arsenite;galectin-1;CD
    Date: 2002-07-08
    Issue Date: 2009-09-22 10:16:47 (UTC+8)
    Publisher: 國立中央大學圖書館
    Abstract: Galectin-1蛋白是一種b-半乳糖苷結合蛋白,其參與細胞貼附、分化及生長調控。Gal-1具有6個還原態的硫氫基,此官能基和蛋白質之lectin活性有直接的關係,但是Gal-1在形成二聚體的過程,並無硫氫基的參與。由近年的研究指出,氧化態Gal-1喪失其lectin活性,但在低濃度下,可促使神經細胞再生及使細胞轉化。由實驗室初步結果顯示,As3+可和Gal-1上的硫氫基結合,並且造成Gal-1的氧化,而此種氧化態Gal-1,運用其生物性功能來影響CHOA細胞;而轉殖Gal-1基因的哺乳類動物細胞,會累積且吸收較多的砷化物。我們利用大腸桿菌系統純化Gal-1和Gal-As3+;並以CD觀察蛋白質,發現gal-As3+在200~205 nm之間有一負值訊號,而gal-1則在205~210nm之間有一負值訊號。由CD值位移的結果間接顯示,亞砷酸鈉 (As3+)和gal-1結合,導致蛋白質二級結構的改變。而由恆溫滴定微卡計的試驗結果得知,亞砷酸鈉滴入gal-1蛋白溶液中的吸附焓介於-55~-69 (kJ/mole As3+)之間。顯示亞砷酸鈉和gal-1之間的作用能量已超過配位鍵的範圍 (~21 kJ/mole)。由初步的結果得知,gal-As3+失去部分lectin活性,且影響HFW細胞的存活率。 Galectin-1 (gal-1), a b-galactoside binding protein, functions in cell adhesion, development, and growth regulation. Gal-1 has six free sulfhydryl groups, which are essential for their lectin property and do not involve in the formation of dimeric gal-1. Recent studies suggest that oxidized gal-1 loses the lectin activity, however, promotes axonal regeneration and cell transformation. We propose that As+3 binds gal-1 through sulfhydryl groups and results in oxidation of gal-1; thereafter, this oxidized gal-1 exerts its biological effect in CHOA cells. Our current results also suggest that gal-1-transfected mammalian cells uptake and accumulate more As3+. The gal-1 and gal-As3+ complexes were prepared from the cell extracts of gal-1-transfected E. coli. The circular dichroism (CD) spectrum of gal-As3+ exhibited a negative signal around 200-205 nm, whereas that of the gal-1 showed a negative signal around 205-210 nm. This shift in the CD spectrum is indicative of a substantial change in secondary structure resulted from the binding of As3+ to gal-1 proteins. Furthermore, the Isothermal titration microcalometric (ITC)studies showed that the absorption enthalpy (△Habs) of As3+ titration into gal-1 protein solution is around –55~-69 kJ/mole As3+. These adsorption enthalpy is high enough for As3+ and gal-1 to form a coordination compounds (~21 kJ/mole). The current results also showed that the gal-As3+ complexes lose partially the lectin activity and effect the cell survival of HFW cells.
    Appears in Collections:[生命科學研究所 ] 博碩士論文

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