資料載入中.....
|
請使用永久網址來引用或連結此文件:
http://ir.cmu.edu.tw/ir/handle/310903500/30522
|
| 題名: | Mutation in the FGFR2 gene in a Taiwanese patient with Beare-Stevenson cutis gyrata syndrome |
| 作者: | Wang, TJ;Huang, CB;Tsai, FJ;Wu, JY;Lai, RB;Hsiao, M |
| 貢獻者: | 附設醫院醫研部;Kaohsiung Chang Gung Mem Hosp, Dept Paediat, Niao Sung Hsiang, Kaohsiung Hsien, Taiwan;China Med Coll Hosp, Dept Paediat, Taichung, Taiwan;China Med Coll Hosp, Dept Med Res, Taichung, Taiwan;Kaohsiung Chang Gung Mem Hosp, Dept Plast Surg, Kaohsiung, Taiwan;Kaohsiung Vet Gen Hosp, Dept Med Educ & Res, Kaohsiung, Taiwan |
| 日期: | 2002 |
| 上傳時間: | 2010-09-24 14:56:58 (UTC+8) |
| 出版者: | BLACKWELL MUNKSGAARD |
| 摘要: | The pseudorabies virus (PRV) DNase is an alkaline exonuclease and endonuclease, which exhibits an Escherichia coli RecBCD-like catalytic function. The PRV DNA-binding protein (DBP) promotes the renaturation of complementary single strands of DNA, which is an essential function for recombinase. To investigate the functional and physical interactions between PRV DBP and DNase, these proteins were purified to homogeneity. PRV DBP stimulated the DNase activity, especially the exonuclease activity, in a dose-dependent fashion. Acetylation of DBP by acetic anhydride resulted in a loss of DNA-binding ability and a 60% inhibition of the DNase activity, suggesting that DNA-binding ability of PRV DBP was required for stimulating the DNase activity. PRV DNase behaved in a processive mode; however, it was converted into a distributive mode in the presence of DBP, implying that PRV DBP stimulated the dissociation of DNase from DNA substrates. The physical interaction between DBP and DNase was further analyzed by enzyme-linked immunosorbent assay, and a significant interaction was observed. Thus, these results suggested that PRV DBP interacted with PRV DNase and regulated the DNase activity in vitro. (C) 2002 Elsevier Science (USA). All rights reserved. |
| 關聯: | CLINICAL GENETICS 61(3):218-221 |
| 顯示於類別: | [台中附設醫院] 期刊論文
|
在CMUR中所有的資料項目都受到原著作權保護.
|
