頁籤選單縮合
| 題 名 | Complex Formation between a Formyl Peptide and 24p3 Protein with a Blocked N-Terminus of Pyroglutamate |
|---|---|
| 作 者 | Chu,Sin-tak; Lin,Han-jia; Chen,Yee-hsiung; | 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183-186 |
| 分類號 | 361.4 |
| 關鍵詞 | Fluorescence; Formyl peptide; 24p3 protein; Pyroglutamate; Pyroglutamate amino peptidase; |
| 語 文 | 英文(English) |
| 英文摘要 | We have purified 24p3 protein from mouse uterine fluid (Biochem. J. 316, 545-550, 1996). It is a 25.8-kDa glycoprotein with a N-blocked terminus. This work demonstrated the N-blocked residue to be pyrogluta-mate, supporting the post-translational cleavage site at Ala-Gln in the precursor protein to generate a putative protein of 180 amino acid residues. Consequently, the two cysteines, Cys□ and Cys□ ,and the two tryptophans, Trp□ and Trp□ , are assigned along the polypeptide chain. No free thiol group was detected in the protein. The presence of formyl-Met-Leu- Phe in the protein solution causes a considerable decrease in the protein fluorescence due to Trp□ and Trp□ . Analysis of the fluorescence date supports the idea that the protein can be complexed with the formyl peptide. The association constant for the complex formation is (4.8±0.29)×10□M□ at Ph 7.4. |
本系統中英文摘要資訊取自各篇刊載內容。