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  2. Transferrin - Wikipedia

    en.wikipedia.org/wiki/Transferrin

    Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein. [7] [8] Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h).

  3. Total iron-binding capacity - Wikipedia

    en.wikipedia.org/wiki/Total_iron-binding_capacity

    It means that transferrin has the capacity to transport approximately from 1.40 to 1.49 mg of iron per gram of transferrin present in the blood. [ 2 ] It is performed by drawing blood and measuring the maximum amount of iron that it can carry, which indirectly measures transferrin [ 3 ] since transferrin is the most dynamic carrier.

  4. Latent iron deficiency - Wikipedia

    en.wikipedia.org/wiki/Latent_Iron_Deficiency

    In spite of an increased level of transferrin, serum iron level is decreased along with transferrin saturation. Erythropoiesis impairment begins when the serum iron level falls to less than 50 μg/dL and transferrin saturation is less than 16%. [4] Stage 3 – Anemia (reduced hemoglobin levels) is present but red blood cell appearance remains ...

  5. Iron in biology - Wikipedia

    en.wikipedia.org/wiki/Iron_in_biology

    At the bone marrow, transferrin is reduced from Fe 3+ and Fe 2+ and stored as ferritin to be incorporated into hemoglobin. [ 5 ] The most commonly known and studied bioinorganic iron compounds (biological iron molecules) are the heme proteins : examples are hemoglobin , myoglobin , and cytochrome P450 . [ 1 ]

  6. Iron-binding proteins - Wikipedia

    en.wikipedia.org/wiki/Iron-binding_proteins

    Iron-binding proteins are carrier proteins and metalloproteins that are important in iron metabolism [1] and the immune response. [2] [3] Iron is required for life.Iron-dependent enzymes catalyze a variety of biochemical reactions and can be divided into three broad classes depending on the structure of their active site: non-heme mono-iron, non-heme diiron , or heme centers. [4]

  7. Transferrin saturation - Wikipedia

    en.wikipedia.org/wiki/Transferrin_saturation

    Transferrin saturation (TS), measured as a percentage, is a medical laboratory value. It is the value of serum iron divided by the total iron-binding capacity [1] of the available transferrin, the main protein that binds iron in the blood, this value tells a clinician how much serum iron is bound. For instance, a value of 15% means that 15% of ...

  8. Serum iron - Wikipedia

    en.wikipedia.org/wiki/Serum_iron

    Serum iron is a medical laboratory test that measures the amount of circulating iron that is bound to transferrin and freely circulate in the blood. Clinicians order this laboratory test when they are concerned about iron deficiency, which can cause anemia and other problems. 65% of the iron in the body is bound up in hemoglobin molecules in red blood cells.

  9. Human iron metabolism - Wikipedia

    en.wikipedia.org/wiki/Human_iron_metabolism

    Most cell types take up iron primarily through receptor-mediated endocytosis via transferrin receptor 1 (TFR1), transferrin receptor 2 (TFR2) and GAPDH. TFR1 has a 30-fold higher affinity for transferrin-bound iron than TFR2 and thus is the main player in this process.