頁籤選單縮合
題名 | The Role of the N-Terminal Leucine Residue in Snake Venom Cardiotoxin Ⅱ (Naja Naja Atra) |
---|---|
作者姓名(外文) | Wu,Chi-yue; Chen,Wan-chen; Ho,Chewn-lang; Chen,Shui-tein; Wang,Kung-tsung; | 書刊名 | 中央研究院生物化學研究所論文集 |
卷期 | 23 1997[民86.] |
頁次 | 頁197-200 |
分類號 | 361.4 |
關鍵詞 | |
語文 | 英文(English) |
英文摘要 | The N-terminal leucine residue of snake venom cardiotoxin II (CTX II) (Naja naja atra) was systematically replaced with D-leucine (CTXII-L1-D-L), glycine (CTXII-L1G) or deleted [CTXII-(2-60) to study the role of leucine residue in CTX II molecule. CTX II, CTXL1-D-L, CTXL1G and CTX(2-60) were produced by chemical synthesis method and purified by high performance liquid chromatography. Owing to folding prob-lem in CTXII-(2-60), only CTX II, CTXII-L1-D-L and CTXII-L1G were produced in a pure form and characterized by amino acid analysis, mass spectrometry and peptide mapping. In the structural aspect, changing the Leu-1 by D- Leu or Gly causes a drastic alteration in the whole CTX II structure as detected by circular dichro- ism, 1-anilino-naphthalene-8-sulfonate (ANS) fluorescence assay. In the functional aspect, both CTXII-L1-D-L and CTXII-L1G are still retained substantial biological activity of CTX II. Therefore, the results indicate that both the chirality and the side-chain of the N-terminal leucine residue of CTX II are important elements in maintaining the whole CTX II structure. In addition, this study is the first report in elucidating the reason why the first N-terminal residue of most CTSs (90.3%) is leucine residue. |
本系統之摘要資訊系依該期刊論文摘要之資訊為主。