Structural specificity of haemosiderin iron cores in iron-overload diseases
Autor: | Dominic P. E. Dickson, Roberta J. Ward, N. M. K. Reid, T. J. Peters, M J O'Connell, Stephen Mann, Vanessa J. Wade |
---|---|
Rok vydání: | 1988 |
Předmět: |
Pathology
medicine.medical_specialty Iron Iron-core structure Biophysics Hemosiderin Biochemistry Ferric Compounds Ferrihydrite Structural Biology Secondary haemochromatosis Genetics medicine Humans Iron-overload Molecular Biology Clinical treatment Oxalates biology Chemistry Oxalic Acid Metallurgy Proteins Cell Biology Primary haemochromatosis Ferritin Spectrometry Gamma Microscopy Electron Liver Solubility Ferritins biology.protein Electrophoresis Polyacrylamide Gel Hemochromatosis Crystallization Dialysis Spleen |
Zdroj: | FEBS letters. 234(1) |
ISSN: | 0014-5793 |
Popis: | Haemosiderin iron cores isolated from patients with secondary haemochromatosis have a goethite-like (α-FeOOH) crystal structure whereas those from patients with primary haemochromatosis are amorphous Fe (III) oxide. Haemosiderin cores isolated from normal human spleen are crystalline ferrihydrite (5Fe2O3·9H2O). The disease-specific structures are significantly different from the ferrihydrite structure of associated ferritin cores. The results are important in understanding the biological processing of iron in pathological states and in the clinical treatment of iron-overload diseases. |
Databáze: | OpenAIRE |
Externí odkaz: |