By P., HARRISON, P.M. et al. AISEN
Chapter 1 a few Physicochemical elements 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 respiration 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: diversified 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 regulate 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 practical 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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Extra info for Ciba Foundation Symposium 51 - Iron Metabolism
Mol. B i d . 14,458473 S. & HAHN,P. (1944) Ferritin V111. Speed and uptake of iron by the liver and its GRANICK, conversion to ferritin iron. J . Biol. G. , HOY:T . G . & MACARA, structure and function, in /roil iii Biucliernistry arid Mediciiie (Jacobs, A. ), pp. 73-1 14, Academic Press, London P. M. & HOY,T. G. (1975) Structure of horse spleen apoferritin at 6 A HOARE, R . , HARRISON, resolution. ) 255,653-654 I . , HAZARD, J. & DRYSDALE, J. W. , LISTOWSKY, position and iron content of isoferritins.
G. & HARRISON, ferritin-catalytic action of apoferritin. Biuclierii. J . 135, 343-348 J . M. H. & COWLEY, of Iron Storage arid Trmiisport in Biocheinistry arid Medicine (Crichton, R. ), pp. , LITT,1. & SHORR,E. (1950) Chemical properties of ferritin and their relation to its vasodepressor activity. J . Biol. Clierii. , FRIEDEN, E. & OSAKI,S. (1974) The release of iron from horse spleen ferritin by SIRIVECH, reduced flavins. Biucliern. J . R. , KOCH, M . H . J . & CRICHTON, scattering of ferritin and apoferritin, in Proteiiis of Iruii Storage t i r i d Trarisport in Biuchemistry and Mediciiie (Crichton.
Even though this suggests that they represent different gene products, the possibility cannot be excluded that they are directly related. For instance, the L subunit might be derived from the H subunit by a specific proteolyticclip, then subsequently modified to give what appear to be the unique peptides. More definitive conclusions await detailed analyses of the unique peptides. VARIATIONS IN ISOFERRITIN PROFILES Although most tissues have a characteristic isoferritin profile in normal adults, these patterns alter markedly in development and in disease states such as iron overload and cancer.
Ciba Foundation Symposium 51 - Iron Metabolism by P., HARRISON, P.M. et al. AISEN