| DC 欄位 |
值 |
語言 |
| DC.contributor | 生命科學系 | zh_TW |
| DC.creator | 黃琦斐 | zh_TW |
| DC.creator | Chi-Fei Huang | en_US |
| dc.date.accessioned | 2002-7-26T07:39:07Z | |
| dc.date.available | 2002-7-26T07:39:07Z | |
| dc.date.issued | 2002 | |
| dc.identifier.uri | http://ir.lib.ncu.edu.tw:88/thesis/view_etd.asp?URN=89224003 | |
| dc.contributor.department | 生命科學系 | zh_TW |
| DC.description | 國立中央大學 | zh_TW |
| DC.description | National Central University | en_US |
| dc.description.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。 | zh_TW |
| dc.description.abstract | 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. | en_US |
| DC.subject | 亞砷酸鈉 | zh_TW |
| DC.subject | 固相結合試驗 | zh_TW |
| DC.subject | solid phase binding assay | en_US |
| DC.subject | ITC | en_US |
| DC.subject | arsenite | en_US |
| DC.subject | galectin-1 | en_US |
| DC.subject | CD | en_US |
| DC.title | 亞砷酸鈉與Galectin-1蛋白交互作用之研究 | zh_TW |
| dc.language.iso | zh-TW | zh-TW |
| DC.title | The study of interaction of arsenite and galectin-1 | en_US |
| DC.type | 博碩士論文 | zh_TW |
| DC.type | thesis | en_US |
| DC.publisher | National Central University | en_US |