Study of the Binding of Iron and Indium to Human Serum Apo-Transferrin

نویسندگان

  • Ali Asghar Moshtaghie
  • Mohammad Ali Ghaffari
چکیده

Indium is a heavy metal belonging to group IIIa. It is believed that indium may interfere with iron metabolism from the sites of absorption, transportation, utilization and storage in the cells. The present investigation was established to study and compare the binding of iron and indium to human apo-transferrin (apo-tf). Pure human apo-tf was used and the binding activity of iron and indium, as a complex with citric acid (1:20), to apo-tf was studied. The binding of iron and indium to apo-tf in TrisHCl buffer, pH 7.4 showed a maximum absorbance at 465 and 255 nm, respectively. The binding of both metals to apo-tf appears to be pH dependent. Using equilibrium dialysis technique, the binding of iron to apo-tf and the effect of indium on the binding process w ere also studied. Addition of indium to the outside of dialysis sac reduced iron uptake by 37%. The results indicate that indium competes with iron in binding to apo-tf. Although, the binding sites for these two ions seem to be similar, the binding of iron to apo-tf is more tightly than indium. Iran. Biomed. J. 7 (2): 73-77, 2003

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Study of the Binding of Iron and Indium to Human Serum Apo-Transferrin

Indium is a heavy metal belonging to group IIIa. It is believed that indium may interfere with iron metabolism from the sites of absorption, transportation, utilization and storage in the cells. The present investigation was established to study and compare the binding of iron and indium to human apo-transferrin (apo-tf). Pure human apo-tf was used and the binding activity of iron and indium, a...

متن کامل

Identification of Amino Acids Involve in Indium Binding To Serum Human Apo-Transferrin

Indium is a heavy metal belonging to group IIIa. It is used as a radioimaging and chemotherapeutic agent in diagnosis and also in the treatment of cancers. It is believed that indium may interfere with iron metabolism and reduce cell growth in cancer tissue. The present report was established to study the binding of iron and indium to apo-transferrin (apo-tf) and to identify amino acids involv...

متن کامل

Manganese and Iron Binding to Human Transferrin

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 contai...

متن کامل

Manganese and Iron Binding to Human Transferrin

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 contai...

متن کامل

Study of Nonenzymatic Glycation of Transferrin and its Effect on Iron -Binding Antioxidant Capacity

Objective(s) Nonenzymatic glycosylation (glycation) occurs in many macromolecules in aging and diabetes due to exposure of biomolecules to high level of glucose. Glycation can changes function, activities and structure of many biomolecules. Considering this important role of transferrin (Trf) in iron transport and antioxidant activity in plasma this study was carried out to investigate the eff...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:

دوره   شماره 

صفحات  -

تاریخ انتشار 2007