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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). Transferrin has a molecular weight of around 80 kDa and contains two specific high-affinity Fe(III) binding sites.
Resultant shifts in electrophoretic migration help distinguish and characterize glycoforms, i.e. variants of a glycoprotein differing in carbohydrate. Compositional analysis following acid hydrolysis: Identifies sugars that the glycoprotein contains and their stoichiometry. Mass spectrometry
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The primary sequence of ovotransferrin is similar to that of many serum transferrins found in other species. Recently, scientists have discovered a blood serum transferrin in humans, that binds iron like ovotransferrin and which shows 50% homology to ovotransferrin, i.e., they have similar amino acid composition and carbohydrate content. At the ...
Beta-2 transferrin is a carbohydrate-free isoform of transferrin, which is almost exclusively found in the cerebrospinal fluid. It is not found in blood , mucus or tears , thus making it a specific marker of cerebrospinal fluid, applied as an assay in cases where cerebrospinal fluid leakage is suspected.
Total iron-binding capacity (TIBC) or sometimes transferrin iron-binding capacity is a medical laboratory test that measures the blood's capacity to bind iron with transferrin. [1] Transferrin can bind two atoms of ferric iron (Fe 3+ ) with high affinity.
Lactoferrin (LF), also known as lactotransferrin (LTF), is a multifunctional protein of the transferrin family. Lactoferrin is a globular glycoprotein with a molecular mass of about 80 kDa that is widely represented in various secretory fluids, such as milk, saliva, tears, and nasal secretions.
In enzymology, a diferric-transferrin reductase (EC 1.16.1.2) is an enzyme that catalyzes the chemical reaction. transferrin[Fe(II)]2 + NAD + + H + transferrin[Fe(III)]2 + NADH. The 3 substrates of this enzyme are [[transferrin[Fe(II)]2]], NAD +, and H +, whereas its two products are [[transferrin[Fe(III)]2]] and NADH.