Transferrin
نویسندگان
چکیده
منابع مشابه
Heterotypic interactions between Transferrin Receptor and Transferrin
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متن کاملManganese 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 کاملManganese 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 کاملTransferrin receptor 2 mediates uptake of transferrin-bound and non-transferrin-bound iron.
BACKGROUND/AIMS Transferrin receptor 2 appears to have dual roles in iron metabolism; one is signalling, the other is iron transport. It is sensitive to high levels of diferric transferrin, which is associated with disorders of iron overload. Also present in these disorders are increased levels of plasma non-transferrin-bound iron. This study sought to clarify the role of transferrin receptor 2...
متن کاملDiferric transferrin regulates transferrin receptor 2 protein stability.
Transferrin receptor 2 (TfR2) is a type 2 transmembrane protein expressed in hepatocytes that binds iron-bound transferrin (Tf). Mutations in TfR2 cause one form of hereditary hemochromatosis, a disease in which excessive absorption of dietary iron can lead to liver cirrhosis, diabetes, arthritis, and heart failure. The function of TfR2 in iron homeostasis is unknown. We have studied the regula...
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ژورنال
عنوان ژورنال: Nature
سال: 1971
ISSN: 0028-0836,1476-4687
DOI: 10.1038/229435b0