Aluminum site structure in serum transferrin and lactoferrin revealed by synchrotron radiation X-ray spectroscopy
Aluminum site structure in serum transferrin and lactoferrin revealed by synchrotron radiation X-ray spectroscopy
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同步辐射X射线光谱揭示血清转铁蛋白和乳铁蛋白中的铝位点结构
DOI:
10.1023/a:1018345021238
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发表时间:
1997
期刊:
影响因子:
3.5
通讯作者:
A. Bianconi
中科院分区:
文献类型:
--
作者:
A. Congiu;F. Boffi;S. Della Longa;A. Giovannelli;M. Girasole;F. Natali;M. Pompa;A. Soldatov;A. Bianconi
The Al site structure of serum transferrin and lactoferrin is investigated using X-ray absorption near edge structure (XANES) spectroscopy. Al K-edge spectra in the mono- and dialuminum forms of the proteins have been recorded for the first time. Our results show that the aluminium ion is hexa-coordinated in an octahedral-like symmetry and that the monoaluminum form, where only the C-terminal binding site is saturated, has an increased structural distortion around the metal site.
DOI:
10.1073/pnas.87.22.9024
发表时间:
1990-11
影响因子:
11.1
作者:
A. J. Roskams;J. Connor
通讯作者:
A. J. Roskams;J. Connor
影响因子:
3.9
作者:
BAKER, EN;LINDLEY, PF
通讯作者:
LINDLEY, PF
DOI:
--
发表时间:
1986
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Thompson,CP;Grady,JK;Chasteen,ND
通讯作者:
Chasteen,ND