Transfer of Iron From Serum Iron-Binding Protein to Human Reticulocytes*

Iron and Protein Kinetics Studied by Means of Doubly Labeled Human Crystalline Transferrin*

“…Recent evidence has suggested that it may play an important part in the control of absorption of iron from the gut (44). Furthermore, the interaction of the protein at specific cellular sites may determine the distribution and chemical form of the iron incorporated into such tissues as marrow and liver (45,46). The studies presented herein indicate that the protein moiety of the transferrin-Fe complex can be labeled with radioiodine without changing its binding properties in vitro.…”

Structure determination of the single glycan of rabbit serotransferrin by methylation analysis and 360 MHz 1H NMR spectroscopy

“…This structure is identical to that of glycan chains of human STF [8, 9,11]. On the basis of the molar carbohydrate composition (table 1) it has to be concluded that the glycoprotein contains only 1 glycan ch~n~mole~ule, which is in contrast to human STF containing 2 glycan chains/molecule of glycoprotein.…”

Macrophages and iron trafficking at the birth and death of red cells

“…Those studies demonstrated that radioactive iron was taken up directly from the plasma, that transferrin was recycled after incorporation of iron into developing reticulocytes, and that a membrane-bound transferrin receptor was required for the process. [20][21][22][23][24][25] The transferrin-iron-transferrin receptor cycle has been extensively studied, showing that diferric transferrin binds the transferrin receptor (also known as CD71) and is internalized via receptormediated endocytosis. Iron is released from transferrin following acidification of the endosome, where it can be mobilized for use in the cell, for storage in ferritin, or for export from the cell.…”