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Isolation and characterization of ferritin from the hepatopancreas of the musselMytilus edulis
Journal article   Peer reviewed

Isolation and characterization of ferritin from the hepatopancreas of the musselMytilus edulis

N. Bootsma, D.J. Macey, J. Webb and V. Talbot
Biology of Metals, Vol.1(2), pp.106-111
1988
DOI: https://doi.org/10.1007/BF01138068
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Abstract

The main iron-binding protein in the hepatopancreas of the mussel Mytilus edulis, which had been previously iron-loaded by exposure to carbonyl iron (spheres of elemental iron less than 5 μm diameter), has been isolated to electrophoretic purity and identified as ferritin. This ferritin has Mr, of 480000, pI of 4.7-5.0 and is composed of two subunits, Mr 18500 and Mr 24600. Under the electron microscope, it appears as electron-dense iron cores of average diameter 5 nm surrounded by a polypeptide shell to a final average overall diameter of 11 nm. The purified protein contains, on average, 200 iron atoms/molecule protein. On immunodiffusion, M. edulis hepatopancreas ferritin gives a partial cross-reaction with antiserum to horse spleen ferritin and lamprey (Geotria australis) liver ferritin but does not react with antiserum to chiton (Acanthopleura hirtosa) haemolymph ferritin.

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