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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.
[17] [18] The higher order multifunctional glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GAPDH) also acts as a transferrin receptor. [19] [20] Transferrin-bound ferric iron is recognized by these transferrin receptors, triggering a conformational change that causes endocytosis. Iron then enters the cytoplasm from the endosome via ...
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.
A glycoprotein is a compound containing carbohydrate (or glycan) covalently linked to protein. The carbohydrate may be in the form of a monosaccharide, disaccharide(s), oligosaccharide(s), polysaccharide(s), or their derivatives (e.g. sulfo- or phospho-substituted). One, a few, or many carbohydrate units may be present.
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 ...
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.
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+ ...
Physical and chemical properties of the drug. The physical properties are solid, liquid and gas. The chemical properties are solubility, stability, pH, irritancy etc. Site of desired action: the action may be localised and approachable or generalised and not approachable. Rate of extent of absorption of the drug from different routes.