Structure and composition of ferritin cores isolated from human spleen, limpet ( Patella vulgata) hemolymph and bacterial ( Pseudomonas aeruginosa) cells

• Published in: Journal of molecular biology Vol. 188; no. 2; pp. 225 - 232
• Main Authors: Mann, Stephen, Bannister, Joseph V., Williams, Robert J.P.
• Format: Journal Article
• Language: English
• Published: Oxford Elsevier Ltd 20.03.1986; Elsevier
• Subjects: Analytical, structural and metabolic biochemistry; Animals; Binding and carrier proteins; Biological and medical sciences; ferritin; Ferritins - analysis; Ferritins - blood; Fundamental and applied biological sciences. Psychology; hemolymph; Hemolymph - analysis; Hemosiderin - analysis; Humans; Microscopy, Electron; Mollusca - analysis; Patella vulgata; Proteins; Pseudomonas aeruginosa; Pseudomonas aeruginosa - analysis; spleen; Spleen - analysis; Pseudomonadales; Human; Spleen; Molecular structure; Ferritin; Hemolymph; Patella vulgata; Vertebrata; Mammalia; Pseudomonadaceae; Bacteria; Pseudomonas aeruginosa; Chemical composition; Comparative study
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/0022-2836(86)90307-4

Ferritin cores isolated from human spleen, limpet ( Patella vulgata) hemolymph and bacterial ( Pseudomonas aeruginosa) cells have been investigated by high resolution transmission electron microscopy, electron diffraction and chemical analysis. Hemosiderin particles isolated from thalassemic spleens also have been studied. The results show that there is a marked difference in structure and composition of the biomineral phases. Human ferritin and hemosiderin particles are single domain crystals of hydrated iron (III) oxide (ferrihydrite). Lattice fringes were low in contrast and often discontinuous within the central regions of the core. Heat treatment of human ferritins results in a 5 Å shrinkage in particle size and an increase in the single crystalline nature of the core. In contrast, lattice images and electron diffraction of limpet and bacterial cores show no evidence of long-range crystallographic order. Chemical analysis indicates a high inorganic phosphate (P i) ( Fe P i = 1.71 ) content in bacterial ferritin compared with human ferritin (thalassemic) ( Fe P i = 21.0 ). The high P i content of bacterial ferritin suggests a hydrated amorphous iron (III) phosphate mineral core. Structural disorder within the limpet and bacterial cores may be associated with increased P i content and increased oxidation in Fe(II), resulting in rapid mineral deposition. Growth of the iron (III) oxide cores in human ferritin is discussed on the basis of high resolution electron microscopy results.