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論文名稱(外文):The study of interation of arsenit and galectin-1
外文關鍵詞:CDITCsolid phase binding assayarsenitegalectin-1lectin activity
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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。
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