By P., HARRISON, P.M. et al. AISEN
Chapter 1 a few Physicochemical facets of Iron Metabolism (pages 1–18): Philip Aisen
Chapter 2 The constitution and serve as of Ferritin (pages 19–40): Pauline M. Harrison, Stephen H. Banyard, Richard J. Hoare, Susan M. Russell and Amyra Treffry
Chapter three Ferritin Phenotypes: constitution and Metabolism (pages 41–78): James W. Drysdale
Chapter four Iron Centres and Rate?Limiting Spans within the breathing Chains of Mitochondria from grownup and Fetal Rats (pages 79–90): Harold Baum and J. ok. Pollak
Chapter five An Intracellular Transit Iron Pool (pages 91–106): Allan Jacobs
Chapter 6 Siderophores: various Roles in Microbial and Human body structure (pages 107–124): J. B. Neilands
Chapter 7 Transferrin: body structure and serve as in Iron delivery (pages 125–144): Elmer B. Brown
Chapter eight Iron Kinetics and Erythropoiesis (pages 145–166): C. Ricketts and that i. Cavill
Chapter nine keep watch over of Iron supply to Haemoglobin in Erythroid Cells (pages 167–200): Premysl Ponka, Jan Neuwirt, Jitka Borova and Ota Fuchs
Chapter 10 Biogenic Monoamine Metabolism and useful task in Iron?Deficient Rats: Behavioural Correlates (pages 201–225): M. B. H. Youdim and A. R. Green
Chapter eleven Monoamine Metabolism and Platelet functionality in Iron?Deficiency Anaemia (pages 227–248): H. F. Woods, M. B. H. Youdim, D. Boullin and S. Callender
Chapter 12 Iron prestige, Immune reaction and Susceptibility to an infection (pages 249–268): R. okay. Chandra, B. Au, G. Woodford and P. Hyam
Chapter thirteen Haem Synthesis in Sideroblastic Anaemia (pages 269–292): A. V. Hoffbrand and L. Konopka
Chapter 14 The Liver in Thalassaemia significant: Ultra?Structural Observations (pages 293–316): T. C. Iancu, H. B. Neustein and B. H. Landing
Chapter 15 Lysosomal Disruption within the Pathogenesis of Hepatic harm in basic and Secondary Haemochromatosis (pages 317–329): T. J. Peters, Clare Selden and Carol A. Seymour
Chapter sixteen Iron, Zinc, loose Radicals and Oxygen in Tissue issues and melanoma regulate (pages 331–369): R. L. Willson
Chapter 17 Chairman's final reviews (pages 371–373): Allan Jacobs
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Additional info for Ciba Foundation Symposium 51 - Iron Metabolism
Bioclieni. Suc. Trans. W. & MUNRO,H . N . (1966) Regulation of synthesis and turnover of ferritin in rat liver. J . B i d . Clierii. T. & BROOKS, D. (1975) Isoferritins in DRYSDALE, J. ~ uiid Metlicitie (Crichton, R. ), pp. 359-366, North-Holland, Amsterdam J . T. DRYSDALE, & YOKOTA, M . ( 1977) Human isoferritins in normal and diseased states. Seriiiii. Hueriiurol. 14. 71-88 FARRANT, J. L. (1954) An electron microscopic study of ferritin. Eiorhirii. W. A. & ANDEREGG, ferritin. J . Mol. B i d .
Harrison: Yes, but in reverse. We took native ferritin and fractionated it to obtain a molecule which is about 257< full. Then we added labelled iron, as Fe(I1). When the iron was released, the labelled iron came out before the unlabelled iron (Hoy et al. 1974). Some of the phosphate release curves in Fig. 5 also follow a ‘last-in-first-out’ principle. Aisen: Does the ( N b & l l ~ ) ~complex + continue to bind iron? Harrison: We haven’t looked at that. Jacobs: Is it now accepted that there is no ferroxidase activity on the outer lip of the channels (see Fig.
It is not known whether the degree of substitution with the H subunit correlates with the degree of malignancy of the tumour. 0, about 85 % H and 15% L) in the face of increasing concentrations of iron (Arosio et af. 1976), by increasing H subunit synthesis (T. G. Adelman & Drysdale, unpublished results). REGULATION OF SUBUNIT SYNTHESIS Most cells seem to have reserves of iron-poor ferritin which can mop up small influxes of iron (Hoy & Harrison 1975). An excess of iron rapidly stimulates the synthesis of new ferritin molecules (Fineberg & Greenberg 1955).
Ciba Foundation Symposium 51 - Iron Metabolism by P., HARRISON, P.M. et al. AISEN