2000
DOI: 10.1002/1097-458x(200006)38:13<::aid-mrc694>3.0.co;2-z
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Muonium formation and magnetic relaxation in dextran and iron-dextran

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Cited by 6 publications
(11 citation statements)
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“…The complexes are pharmaceutically important as synthetic substitutes for the iron storage protein ferritin, and it is used in the treatment of iron deficiency anaemias (28). Research shows that irondextran complexes are composed of an iron-based core with a dextran shell (27)(28)(29)(30)(31). At the same time, the adsorption of nonionic surfactants on metal oxides is believed to be a physical process through hydrogen bonding and van der Waals attraction force (32).…”
Section: Partitioning Behavior Of Hematite In the Dextran/triton X-10mentioning
confidence: 99%
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“…The complexes are pharmaceutically important as synthetic substitutes for the iron storage protein ferritin, and it is used in the treatment of iron deficiency anaemias (28). Research shows that irondextran complexes are composed of an iron-based core with a dextran shell (27)(28)(29)(30)(31). At the same time, the adsorption of nonionic surfactants on metal oxides is believed to be a physical process through hydrogen bonding and van der Waals attraction force (32).…”
Section: Partitioning Behavior Of Hematite In the Dextran/triton X-10mentioning
confidence: 99%
“…Although both of these surfactants can modify the surface chemistry of ferric oxide at certain pH values in conventional aqueous solutions, neither one changed the partitioning behavior of hematite in this polymer/surfactant system. Since dextran strongly interacts with ferric oxide (27)(28)(29)(30)(31), it appears that SDS or oleate is not able to replace the strongly adsorbed dextran layer on the hematite surface so that the particles continue to stay in the bottom phase.…”
Section: Effects Of Surfactants On Hematite Partitionmentioning
confidence: 99%
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“…The largest biological molecules that appear to have been investigated using MuSR methods are cytochrome c, 74,75 myoglobin 75 and dextran 76 and an iron-dextran complex. 76 In cytochrome c, it is found that muonium is trapped at the oxygen atom of CNO amino acid groups, where the muon relaxation rate is subject to the influence of electronic dynamics; free muons are predicted to associate with all atoms on the protein chain carrying a negative charge, so addition of both muon and Mu is expected at the CNO oxygen sites. In the heme units, muons are trapped at the pyrrole nitrogen atoms, where they are subject to a 'chemical shift' of 88.4 ppm.…”
Section: Measurements Relevant To An Alternative Mode Of Lipid Damagementioning
confidence: 99%