Author/Authors :
Moshtaghie, Ali Asghar Department of Clinical Biochemistry - School of Medicine - Razi University, Kermanshah , Badii, Akbar Department of Clinical Biochemistry - School of Medicine - Razi University, Kermanshah , Fazilati, Mohammad Department of Food Sciences - School of Agricalture - Isfahan University of Technology, Isfahan , Hassanzadeh, Taghi Department of Clinical Biochemistry - School of Medicine - Razi University, Kermanshah , Kharazi, Hadi Department of Clinical Biochemistry - School of Medicine - Razi University, Kermanshah
Abstract :
The characteristics of manganese and iron binding to human apotransferrin (apo-tf) have been investigated and compared in this study. Both metal ions were taken up by human apo-tf and formed complexes, with the maximum absorbances observed at 410 and 340 nm for manganese-transferrin (Mn-tf) and 465 nm for iron-transferrin (Fe-tf). Addition of manganese (1.5 µg/ml) to the reaction mixture containing iron and apo-tf, reduced Fe binding to apo-tf by 20 percent, in comparison to the control sample. The binding of both metals to apo-tf appears to be time and pH dependent processes. Using the equilibrium dialysis technique, the binding constant of manganese to apo-tf was also determined. The binding constatnt of Mn to apo-tf was calculated, using the Scatchard plot analysis. The calculated Ka was 3.1×109 M-1. The binding of manganese and iron to human apo-tf has been discussed and compared in this work, using different biochemical techniques.
Keywords :
Manganese , Iron , Transferrin , Binding activity
