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It is the primary intracellular iron-storage protein in both prokaryotes and eukaryotes, keeping iron in a soluble and non-toxic form. In humans, it acts as a buffer against iron deficiency and iron overload. [3] Ferritin is found in most tissues as a cytosolic protein, but small amounts are secreted into the serum where it functions as an iron ...
Iron–sulfur proteins are proteins characterized by the presence of iron–sulfur clusters containing sulfide-linked di-, tri-, and tetrairon centers in variable oxidation states. Iron–sulfur clusters are found in a variety of metalloproteins , such as the ferredoxins , as well as NADH dehydrogenase , hydrogenases , coenzyme Q – cytochrome ...
These cells have special molecules that allow them to move iron into the body. To be absorbed, dietary iron can be absorbed as part of a protein such as heme protein or iron must be in its ferrous Fe 2+ form. A ferric reductase enzyme on the enterocytes' brush border, duodenal cytochrome B , reduces ferric Fe 3+ to Fe 2+. [27]
Macrophages of the reticuloendothelial system store iron as part of the process of breaking down and processing hemoglobin from engulfed red blood cells. Iron is also stored as a pigment called hemosiderin, which is an ill-defined deposit of protein and iron, created by macrophages where excess iron is present, either locally or systemically, e ...
434624 Ensembl ENSG00000087086 n/a UniProt P02792 n/a RefSeq (mRNA) NM_000146 n/a RefSeq (protein) NP_000137 n/a Location (UCSC) Chr 19: 48.97 – 48.97 Mb n/a PubMed search Wikidata View/Edit Human View/Edit Mouse Ferritin light chain is a protein that in humans is encoded by the FTL gene. Ferritin is the major protein responsible for storing intracellular iron in prokaryotes and eukaryotes ...
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]
The potential role of succinylation is under investigation, but as addition of succinyl group changes lysine's charge from +1 to −1 (at physiological pH) and introduces a relatively large structural moiety (100 Da), bigger than acetylation (42 Da) or methylation (14 Da), it is expected to lead to more significant changes in protein structure ...
This can be done in terms of the chemical elements present, or by molecular structure e.g., water, protein, fats (or lipids), hydroxyapatite (in bones), carbohydrates (such as glycogen and glucose) and DNA. In terms of tissue type, the body may be analyzed into water, fat, connective tissue, muscle, bone, etc.