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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).
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
In human cells, the best-characterized iron-sensing mechanism is the result of post-transcriptional regulation of mRNA (the chemical instructions derived from DNA genes to make proteins). Sequences of mRNA called iron-responsive elements (IREs) are contained within the mRNA sequences that code for transferrin receptors and for ferritin.
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.
Biologically, conalbumin isolates and sequesters metallic contaminants in the egg white. [3] Ovotransferrin is functionally and structurally analogous to mammalian lactoferrin [4] A recent study has shown superior performance of ovotransferrin when compared to lactoferrin in its capability to deliver iron without accumulation or inducing gastric irritability, rendering ovotransferrin as an ...
Ferritin is a much larger protein than transferrin and is capable of binding several thousand iron atoms in a nontoxic form. Siderophores are unable to directly mobilise iron from ferritin. In addition to these two classes of iron-binding proteins, a hormone, hepcidin, is involved in controlling the release of iron from absorptive enterocytes ...
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. This enzyme belongs to the family of oxidoreductases, specifically those oxidizing metal ion with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is transferrin[Fe(II)]2:NAD+ ...
Native chemical ligation (NCL) is a convergent synthetic strategy based on the linear coupling of glycopeptide fragments. This technique makes use of the chemoselective reaction between a N-terminal cysteine residue on one peptide fragment with a thio-ester on the C-terminus of the other peptide fragment [ 19 ] as illustrated below.