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'Electron Spin Resonance' in keywords
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1989 (1)
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1980 (2)
1Author    S. Cannistraro, P. L. Indovina, L. SportelliRequires cookie*
 Title    Paramagnetic Species in /^-Thalassemic Sera: an ESR Study  
 Abstract    Homozygous beta thalassemic sera show an electron spin resonance (ESR) signal at g ~ 6 which is not present in normal and heterozygous sera. The signal arises from high spin heme groups exhibiting a departure from tetragonal symmetry toward rhombic. Binding by a serum protein is very likely responsible for such a distortion. In contrast with other authors' findings, we report that heme-human albumin complex shows a similar rhombic distortion. The observed ESR signal at g ~ 6 is then attributed to this complex. 
  Reference    Z. Naturforsch. 35c, 193—196 (1980); received November 23 1979 
  Published    1980 
  Keywords    Heme Groups, Albumin, ^-Thalassemia, Electron Spin Resonance 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0193.pdf 
 Identifier    ZNC-1980-35c-0193 
 Volume    35 
2Author    PietroL. IndovinaRequires cookie*
 Title      
 Abstract    We describe the appearance of a free-radical signal in the ESR spectrum of normal human serum incubated with several complement activating agents. The intensity o f this signal is dependent of dose of activating agents, time and temperature. Signals elicited by different complement activators differ in morphology and kinetics. Inhibition by treatment with EDTA and the presence o f the signal in activated C 6-deficient rabbit serum suggest that the con-vertase forming steps of complement activation (C2 to 5) could be the source of free-radical containing molecules. 
  Reference    Z. Naturforsch. 35c, 844—847 (1980); received May 12/June 16 1980 
  Published    1980 
  Keywords    Complement, Electron Spin Resonance, Free Radicals 
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 TEI-XML for    default:Reihe_C/35/ZNC-1980-35c-0844_n.pdf 
 Identifier    ZNC-1980-35c-0844_n 
 Volume    35 
3Author    Grzegorz Bartosz, G. Abriele, Christ, Harald Bosse, Roland Stephan, HelmutG. ÄrtnerRequires cookie*
 Title    Thermal Lability of Membrane Proteins of Age Separated Erythrocytes as Studied by Electron Spin Resonance Spin Label Technique  
 Abstract    Thermal lability of bovine erythrocyte membrane pro­ teins was studied by electron spin resonance using maleimide spin label. The temperature of the sample du­ ring measurements could be varied for the first time be­ tween 0 and 60 °C with an accuracy of ± 0.1 °C. Our results show that "old" erythrocyte membrane proteins are less stable against thermal denaturation then "young" cells. 
  Reference    Z. Naturforsch. 42c, 1343—1344 (1987); received March 13/October 16 1987 
  Published    1987 
  Keywords    Membrane Proteins, Erythrocyte Aging, Electron Spin Resonance, Spin Label Technique 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-1343_n.pdf 
 Identifier    ZNC-1987-42c-1343_n 
 Volume    42 
4Author    Robert Schupfner, Adolf MüllerRequires cookie*
 Title    Temperature-Dependent ESR Studies of Radical Pairs in Single Crystals of Barbituric Acid  
 Abstract    After irradiation o f single crystals o f barbituric acid with X-rays at 77 K different types of radical pairs are found, which are com posed o f only one type of monoradical. The properties of radical pairs o f the unpaired electrons are studied using frequency-variable ESR m ethods at various temperatures. In addition to the radical pairs A D and BC two further pairs A 'D ' and X Y were identified. M easurem ents o f the fine structure parameter D showed a linear temperature dependence in som e regions betw een 77 K and 290 K. At 240 K the radical pairs A D and A 'D ' changed reversibly into A *D * and this pair remained stable up to 290 K. A level anticrossing effect was observed with the pair A D . The exchange energy J between the singlet state and the triplet state was determ ined as —(15.1 ± 0.6) GHz at 77 K and its tem pera­ ture coefficient as —(3.8 ± 0.8) x 10"3K '. 
  Reference    Z. Naturforsch. 44c, 849 (1989); received April 20/June 29 1989 
  Published    1989 
  Keywords    Barbituric A cid Single Crystals Radical Pairs, Electron Spin Resonance, Level Anticrossing 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0849.pdf 
 Identifier    ZNC-1989-44c-0849 
 Volume    44 
5Author    JankoN. Herak, Günter BehrensRequires cookie*
 Title    An in-situ Electron Spin Resonance Study  
 Abstract    ESR spectroscopy has been used to analyse the conformation of the radicals produced by the reaction of SOj with D-ribose (1), and 2-deoxy-D-ribose (6), at pH 1.3-5. From ribose three different types of radicals formed by H abstraction at C -l, C-2 and C-3 followed by a regio-selective a,ß-water elimination have been identified: the 2-deoxy-ribonolacton-2-yl (3), the 1-deoxy-pentopyranos-2-ulos-l-yl (4). and the 4-deoxy-pentopyranos-3-ulos-4-yl (2). Using deoxyribose two radicals of similar type, formed by H abstraction at C-3 and C-4 followed by water elimination, have been observed: the 2,4-dideoxy-3-ulos-4-yl (7) and the 2,3-dideoxy-4-ulos-3-yl (8). In addition, from both sugars an a-hydroxyalkyl radical has been identified based in part on the timing of their conformational motions: the ribos-3-yl (5) (the precursor of 2) and the 2-deoxy-ribos-l-yl (9), respectively. For radical 5 the rate constant k(e) for the water elimination and hence transformation into radical 2 was estimated. From the analysis of selective line broadening the frequencies of conformational changes of radicals 2 and 7 have been estimated. For 7 the frequencies of exchange of the two methylene groups were found to differ by more than 3 orders of magnitude. 
  Reference    Z. Naturforsch. 41c, 1062 (1986); received January 31 1986 
  Published    1986 
  Keywords    Free Radicals, Deoxy-D-ribose, D-Ribose, Conformational Kinetics, Electron Spin Resonance 
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 TEI-XML for    default:Reihe_C/41/ZNC-1986-41c-1062.pdf 
 Identifier    ZNC-1986-41c-1062 
 Volume    41