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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 ...
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]
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.
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 ...
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.