@article{
 title = {Electron spin resonance studies of splenic ferritin and haemosiderin.},
 type = {article},
 year = {1985},
 identifiers = {[object Object]},
 keywords = {1-0,2 ghz,2 t,9,approx,at 0,broad features,by electron,composed of two,esr,ferritin,ferritin isolated from iron-loaded,hemosiderin,human spleen,human spleens were studied,its major component occurring,one extremely anisotropic with,overlapping,preparations of haemosiderin and,spectroscopy at x-band,spin resonance,the spectra were mainly},
 pages = {298-305},
 volume = {828},
 id = {b0ee5ba5-dd07-3e52-9f07-45f68b1f0bf4},
 created = {2016-08-07T12:59:48.000Z},
 file_attached = {true},
 profile_id = {5d250c3e-485a-3099-8087-b35242bd2203},
 group_id = {a9625e9e-5a77-317b-ab12-c1d6dcc9ef27},
 last_modified = {2016-09-16T14:52:33.000Z},
 read = {true},
 starred = {false},
 authored = {false},
 confirmed = {true},
 hidden = {false},
 citation_key = {Weir1985a},
 abstract = {Preparations of haemosiderin and ferritin isolated from iron-loaded human spleens were studied by electron spin resonance (ESR) spectroscopy at X-band (approx. 9.2 GHz). The spectra were mainly composed of two overlapping, broad features, one extremely anisotropic with its major component occurring at 0.1-0.2 T (feature A), the other nearly isotropic and occurring at around g = 2 (feature B). There is relatively more feature A and less feature B in ferritin than in haemosiderin. Both features originate from the iron oxyhydroxide crystallites of these iron proteins which, due to their small size, are superparamagnetic. Feature B is maximal in small cores or at high temperatures, where superparamagnetic fluctuations average out anisotropic magnetic interactions; feature A is greatest at low temperatures or in large cores, for which such fluctuations are blocked and an ESR spectrum characteristic of a magnetically ordered system is observed. It is concluded that there is no evidence in the ESR spectra for 'loose' protein-bound Fe3+ in ferritin or haemosiderin, and that haemosiderin cores are on average smaller than those of ferritin. The relationship of the ESR spectra between these two proteins supports the view that haemosiderin is derived from ferritin.},
 bibtype = {article},
 author = {Weir, M P and Peters, T J and Gibson, J F},
 journal = {Biochimica et biophysica acta}
}

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The spectra were mainly composed of two overlapping, broad features, one extremely anisotropic with its major component occurring at 0.1-0.2 T (feature A), the other nearly isotropic and occurring at around g = 2 (feature B). There is relatively more feature A and less feature B in ferritin than in haemosiderin. Both features originate from the iron oxyhydroxide crystallites of these iron proteins which, due to their small size, are superparamagnetic. Feature B is maximal in small cores or at high temperatures, where superparamagnetic fluctuations average out anisotropic magnetic interactions; feature A is greatest at low temperatures or in large cores, for which such fluctuations are blocked and an ESR spectrum characteristic of a magnetically ordered system is observed. It is concluded that there is no evidence in the ESR spectra for 'loose' protein-bound Fe3+ in ferritin or haemosiderin, and that haemosiderin cores are on average smaller than those of ferritin. The relationship of the ESR spectra between these two proteins supports the view that haemosiderin is derived from ferritin.","bibtype":"article","author":"Weir, M P and Peters, T J and Gibson, J F","journal":"Biochimica et biophysica acta","bibtex":"@article{\n title = {Electron spin resonance studies of splenic ferritin and haemosiderin.},\n type = {article},\n year = {1985},\n identifiers = {[object Object]},\n keywords = {1-0,2 ghz,2 t,9,approx,at 0,broad features,by electron,composed of two,esr,ferritin,ferritin isolated from iron-loaded,hemosiderin,human spleen,human spleens were studied,its major component occurring,one extremely anisotropic with,overlapping,preparations of haemosiderin and,spectroscopy at x-band,spin resonance,the spectra were mainly},\n pages = {298-305},\n volume = {828},\n id = {b0ee5ba5-dd07-3e52-9f07-45f68b1f0bf4},\n created = {2016-08-07T12:59:48.000Z},\n file_attached = {true},\n profile_id = {5d250c3e-485a-3099-8087-b35242bd2203},\n group_id = {a9625e9e-5a77-317b-ab12-c1d6dcc9ef27},\n last_modified = {2016-09-16T14:52:33.000Z},\n read = {true},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n citation_key = {Weir1985a},\n abstract = {Preparations of haemosiderin and ferritin isolated from iron-loaded human spleens were studied by electron spin resonance (ESR) spectroscopy at X-band (approx. 9.2 GHz). The spectra were mainly composed of two overlapping, broad features, one extremely anisotropic with its major component occurring at 0.1-0.2 T (feature A), the other nearly isotropic and occurring at around g = 2 (feature B). There is relatively more feature A and less feature B in ferritin than in haemosiderin. Both features originate from the iron oxyhydroxide crystallites of these iron proteins which, due to their small size, are superparamagnetic. Feature B is maximal in small cores or at high temperatures, where superparamagnetic fluctuations average out anisotropic magnetic interactions; feature A is greatest at low temperatures or in large cores, for which such fluctuations are blocked and an ESR spectrum characteristic of a magnetically ordered system is observed. It is concluded that there is no evidence in the ESR spectra for 'loose' protein-bound Fe3+ in ferritin or haemosiderin, and that haemosiderin cores are on average smaller than those of ferritin. The relationship of the ESR spectra between these two proteins supports the view that haemosiderin is derived from ferritin.},\n bibtype = {article},\n author = {Weir, M P and Peters, T J and Gibson, J F},\n journal = {Biochimica et biophysica acta}\n}","author_short":["Weir, M., P.","Peters, T., J.","Gibson, J., F."],"urls":{"Paper":"http://bibbase.org/service/mendeley/1636e51c-ec94-3a34-9257-22309a74bcae/file/5afc5692-a5af-028f-51e3-0d2a4f5fb9ea/1985-Electron_spin_resonance_studies_of_splenic_ferritin_and_haemosiderin..pdf.pdf"},"bibbaseid":"weir-peters-gibson-electronspinresonancestudiesofsplenicferritinandhaemosiderin-1985","role":"author","keyword":["1-0","2 ghz","2 t","9","approx","at 0","broad features","by electron","composed of two","esr","ferritin","ferritin isolated from iron-loaded","hemosiderin","human spleen","human spleens were studied","its major component occurring","one extremely anisotropic with","overlapping","preparations of haemosiderin and","spectroscopy at x-band","spin resonance","the spectra were mainly"],"downloads":0},"search_terms":["electron","spin","resonance","studies","splenic","ferritin","haemosiderin","weir","peters","gibson"],"keywords":["1-0","2 ghz","2 t","9","approx","at 0","broad features","by electron","composed of two","esr","ferritin","ferritin isolated from iron-loaded","hemosiderin","human spleen","human spleens were studied","its major component occurring","one extremely anisotropic with","overlapping","preparations of haemosiderin and","spectroscopy at x-band","spin resonance","the spectra were mainly"],"authorIDs":[]}