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http://ir.cmu.edu.tw/ir/handle/310903500/29344
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| 題名: | Predicting factors associated with costs of diabetic patients in Taiwan |
| 作者: | Lin, T;Chou, PS;Tsai, ST;Lee, YC;Tai, TY |
| 貢獻者: | 附設醫院社區醫學部;Natl Yang Ming Univ, Community Med Res Ctr, Taipei 112, Taiwan;Natl Yang Ming Univ, Inst Publ Hlth, Taipei 112, Taiwan;China Med Univ Hosp, Dept Community Med, Taipei, Taiwan;Vet Gen Hosp, Dept Med, Taipei, Taiwan;Natl Yang Ming Univ, Inst Hlth & Welf Policy, Taipei 112, Taiwan;Natl Taiwan Univ Hosp, Dept Internal Med, Taipei 100, Taiwan |
| 日期: | 2004 |
| 上傳時間: | 2010-09-24 14:32:46 (UTC+8) |
| 出版者: | ELSEVIER SCI IRELAND LTD |
| 摘要: | The conserved cobalamin-binding domain of glutamate mutase exists as a separate dissociable subunit, MutS The results obtained from BIAcore analysis indicate that MutS alone, in the absence of E component of glutamate mutase (MutE, catalytic subunit), is capable of binding hydroxocobinamide (OHCbi) with a K-d of 15.4+/-1.6 muM, but fails to bind adenoslcobalamin (AdoCbl). The UV-visible spectrum indicates that histidine ligation to the cobalt atom only occurs when both MutE and MutS are present in the solution. MutS mutants, MutS-D14N and MutS-H16G, are also capable of binding OHCbi, but their binding kinetics altered. Our experimental results show that the electrostatic interaction between histidine-aspartate pair is important in the binding of OHCbi or AdoCbl, no matter whether histidine coordinates to the cobalt atom or not. The catalytic subunit is also involved in histidine ligation to the cobalt atom. Meanwhile, mutation of either His16 or Asp14 significantly impairs the enzyme to cleave the cobalt-carbon bond of AdoCbl. (C) 2003 Elsevier Ltd. All rights reserved. |
| 關聯: | DIABETES RESEARCH AND CLINICAL PRACTICE 63(2):119-125 |
| 顯示於類別: | [台中附設醫院] 期刊論文
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