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Last Updated: 4 years ago

Possible Interaction: Albumin and Cupric Cation

supplement:

Albumin

supplement:

Cupric Cation

Research Papers that Mention the Interaction

Ultrafiltration studies using solutions of dog and human serum albumin reveal that the 67Cu complexes of ligands 4a-d, like the Cu(II) complex of pyruvaldehyde bis(N4-methylthiosemicarbazone), interact more strongly with human albumin than dog albumin.
Journal of medicinal chemistry  •  1997  |  View Paper
Addition of either serum or albumin significantly reduced the stimulation effect of Cu2+ , and almost completely eliminated that of Fe3+ and Zn2+.
Anticancer research  •  1997  |  View Paper
Exposure of albumin to Cu(II) (10-100 microM) and ascorbate (0.1-2 mM) results in extensive molecular modifications, indicated by decreased fluorescence and chain breaks.
The Biochemical journal  •  1986  |  View Paper
Cp … albumin , modified Cu(II) induced hemolysis, by increasing the duration of the induction period and decreasing the overall rate of hemolysis of RBC.The catastrophic lysis period coincided with a sharp increase in the formation of metHb within the cell and in a rapid uptake of Cu(II).
The hemolysis of red blood cells (RBC) induced by Cu(II) is modified by ceruloplasmin (Cp) and albumin.
Biological Trace Element Research  •  2008  |  View Paper
At higher pH (~9), when the protein is in the basic (B) form, a second Cu(II) binds with high affinity to albumin with reduced Cys-34.
JBIC Journal of Biological Inorganic Chemistry  •  2001  |  View Paper
Albumin markedly inhibited Cu(II) uptake at Cu(II)-to-albumin molar ratios of 3:1 or less.
Kinetic analyses showed that albumin inhibits Cu(II) uptake by reducing the concentration of free Cu(II) in solution.
The American journal of physiology  •  1984  |  View Paper
In a further study, albumin inhibited Cu2+ -induced oxidation of LDL in a stoichiometric manner with an EC50 value of 4.3 microM, close to that of serum albumins.
Taken together, rice albumin exerts a potent preventive action against Cu2+ -induced oxidations, which is due to the Cu2+ binding by DHHQ in the N-terminal sequence.
The rice albumin was more potent than other rice proteins in preventing Cu2+ -induced low-density lipoprotein (LDL) oxidation.
Journal of agricultural and food chemistry  •  2007  |  View Paper