Structural changes of human serum albumin in response to a low concentration of heavy ions.
Structural changes of human serum albumin in response to a low concentration of heavy ions.
复制标题
DOI：
10.1002/jbio.201000044
复制
发表时间：
2010-10
影响因子：
2.8
通讯作者：
Yakovlev, Vladislav V.
中科院分区：
文献类型：
--
作者：
Saha, Anushree;Yakovlev, Vladislav V.
Lead ions in solution interact strongly with human serum albumin and modify the properties and function of albumin molecules. In the present study, we used optical spectroscopic techniques to explore the binding sites of lead, present in albumin. Structural and chemical analysis of albumin molecules using fluorescence and Raman spectroscopy, predicted the modification of two major amino acids in albumin due to lead binding. No secondary structural changes are observed in the protein molecule, which is further confirmed using circular dichroism absorption measurements. The results indicate that loss of charge from the binding site of albumin by the charged lead ions, give rise to dipole interaction which acts as the major contributor to promote protein agglomeration. Stepwise formation of a protein cluster in the presence of a lead ion.
登录
查看更多内容
影响因子：
2.9
作者：
LIN, VJC;KOENIG, JL
通讯作者：
KOENIG, JL
DOI：
10.1111/j.1432-1033.1995.178_c.x
发表时间：
1995-11-15
期刊：
EUROPEAN JOURNAL OF BIOCHEMISTRY
影响因子：
--
作者：
SIMONS, TJB
通讯作者：
SIMONS, TJB
影响因子：
2.7
作者：
Sudhakar, K;Wright, W W;Vanderkooi, J M
通讯作者：
Vanderkooi, J M
影响因子：
15
作者：
Ghering, AB;Jenkins, LMM;Godwin, HA
通讯作者：
Godwin, HA
影响因子：
15
作者：
Payne, JC;ter Horst, MA;Godwin, HA
通讯作者：
Godwin, HA