apoferritin


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apoferritin

 [ap″o-fer´ĭ-tin]
an apoprotein that can bind many atoms of iron per molecule to form ferritin, the form in which iron is stored in the liver and other tissues.

ap·o·fer·ri·tin

(ap'ō-fer'i-tin),
A protein in the intestinal wall that combines with a ferric hydroxide-phosphate compound to form ferritin, the first stage in the absorption of iron. Apoferritin is an oligomer of 24 chains in a spheric structure; the cavity of this sphere can contain up to 4,500 Fe3+ ions.

ap·o·fer·ri·tin

(ap-ō-fer'i-tin)
A protein in the intestinal wall that combines with a ferric hydroxide-phosphate compound to form ferritin, the first stage in the absorption of iron.

apoferritin

A substance with which absorbed iron may be complexed in the body to form a ferritin store. Ferritin is one of the two forms of iron store in the cells of the body. The other is haemosiderin.
References in periodicals archive ?
Method Size/nm Property Bioinspired synthesis 5 Two- or three-dimensional nanoceria by apoferritin coating.
When intracellular iron concentration is low, an iron regulatory protein inhibits the synthesis of apoferritin and promotes the synthesis of transferrin receptor.
The small amount of circulating ferritin is mostly apoferritin that contains little iron.
Vekilov and Siu-Tung Yau at the University of Alabama in Huntsville used an atomic force microscope to view the protein apoferritin as it crystallizes.
To overcome these challenges, Vekilov and Yau waited for apoferritin clusters to approach the bottom of a glass cell where the researchers already had placed an apoferritin crystal as a docking point.
They found that all of these clusters had roughly the same shape--a flat layer of apoferritin molecules with a few more molecules on top.
The equation was derived from the migration distances of both protein-coated gold particles (diameters, 21.1 and 29.2 nm, respectively) and from the migration distances of the thyroglobulin dimer (23.6 nm), thyroglobulin (17.0 nm), and apoferritin (12.2 nm).
Thyroglobulin (T-1126), apoferritin (A-3641), and dithiothreitol (D-0632) were purchased from Sigma.
The average particle diameters of the calibrator LDL samples were estimated by GGE from a linear calibration curve of the logarithm of the diameter vs the migration distance, with apoferritin (12.2 nm), thyroglobulin (17.0 nn), and thyroglobulin dimer (23.6 nm) as calibrators of known diameter.
Marker proteins, e.g., apoferritin and thyroglobulin, and calibrated latex beads are frequently used in GGE for calibration.
Effects of H and L human apoferritins on lipid peroxidation in vitro.