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  • 1
    Electronic Resource
    Electronic Resource
    Nuclear weapons and power-reactor plutonium (1980)
    [s.l.] : Nature Publishing Group
    Nature 283 (1980), S. 817-823 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] With modest design sophistication, high-burn-up plutonium from power reactors can produce powerful and predictable nuclear explosions. There is no way to ‘denature’ plutonium. Power reactors are not implausible but rather attractive as military production reactors. Current promotion of ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/283817a0
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Soft energy paths (1978)
    [s.l.] : Nature Publishing Group
    Nature 271 (1978), S. 107-108 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR,-Peter Chapman is right to say (10 November, page 128) that my US calculations in Soft Energy Paths: Toward a Durable Peace should be redone for the UK-as several colleagues are now attempting. But in suggesting how my US numbers "fail on a number of technical issues" he may mislead UK readers ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/271107b0
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  • 3
    Electronic Resource
    Electronic Resource
    Plutonium and other actinides (1977)
    [s.l.] : Nature Publishing Group
    Nature 265 (1977), S. 390-390 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] THESE 41 technical papers form an indispensable basis for assessing the "growing concern about man's ignorance of the bio geochemistry of [plutonium and other actinides] ... in relation to ... long-term buildup, availability, and transport in the environment" (Noshkin). Nowhere is this concern more ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/265390b0
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  • 4
    Electronic Resource
    Electronic Resource
    Nitrogen fixation (1975)
    [s.l.] : Nature Publishing Group
    Nature 255 (1975), S. 8-8 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR,-Current 'biochemical and geneJtic attempts to develoip nitrogen-fixing bacteria symbiotic with plants now lacking them (some described by John Postgate, Nature, January 31, p. 305) raise a significant question. Sir Peter Medawar has said that when developing a new technology, one should try ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/255008c0
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  • 5
    Electronic Resource
    Electronic Resource
    Energy strategy (1974)
    [s.l.] : Nature Publishing Group
    Nature 247 (1974), S. 332-332 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] SIR,-I am sorry that travel has kept me from responding earlier to your provocative leader 'A Broader Debate on Energy' (Nature, 246, 179; 1973). In kindly discussing my monograph, 'World Energy Strategies: Facts, Issues, and Options', you attempt what I did not dare-a brief summary of an ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/247332a0
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  • 6
    Electronic Resource
    Electronic Resource
    Quantitative Approach to the Sequential Degradation of Proteins and Peptides (1969)
    [s.l.] : Nature Publishing Group
    Nature 221 (1969), S. 1241-1244 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] Fig. 1. Mass spectra of phenylalanine methyl thiohydantoin at (A) 70 eV, (B) 10 eV. Fig. 2. mass spectra of a mixture of amino-acid methyl thiohydantoin derivatives at (I) probe temperature 90?, (II) 140?, (III) 160?, (IV) 200?. Ionizing voltage 10 e V. A, Glycine; B, alanine; C, valine; D, ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/2211241a0
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  • 7
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    Binding of immunoglobulin classes to subpopulations of human red blood cells separated by density-gradient centrifugation (1980)
    American Society of Hematology
    Details
    Publication Date: 1980-05-01
    Description: Human erythrocytes (RBC) from whole blood were separated according to their specific densities by centrifugation on a polyvinyl-pyrrolidine- coated colloidal silica matrix (Percoll) into four major subpopulations. By indirect immunofluorescence assay, the most dense RBC subpopulation, with specific density greater than 1.110 g/ml (3%-5% of total RBC), was positive for membrane-bound immunoglobulin; the remaining, less dense subpopulations were negative. IgG was present on 85%-95%, IgM on 28%-32%, and IgA on 15%-20% of the RBC in the most dense population. When these immunoglobulins were eluted, radiolabeled, and used in binding studies with autologous RBC fractions subjected to thermal and/or enzymatic treatment, they reacted specifically with the less dense RBC subpopulations. These results suggest that previously cryptic antigens were revealed by the activity of neuraminidase on the plasma membranes of the treated RBC.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 8
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    Binding of immunoglobulin classes to subpopulations of human red blood cells separated by density-gradient centrifugation (1980)
    American Society of Hematology
    Details
    Publication Date: 1980-05-01
    Description: Human erythrocytes (RBC) from whole blood were separated according to their specific densities by centrifugation on a polyvinyl-pyrrolidine- coated colloidal silica matrix (Percoll) into four major subpopulations. By indirect immunofluorescence assay, the most dense RBC subpopulation, with specific density greater than 1.110 g/ml (3%-5% of total RBC), was positive for membrane-bound immunoglobulin; the remaining, less dense subpopulations were negative. IgG was present on 85%-95%, IgM on 28%-32%, and IgA on 15%-20% of the RBC in the most dense population. When these immunoglobulins were eluted, radiolabeled, and used in binding studies with autologous RBC fractions subjected to thermal and/or enzymatic treatment, they reacted specifically with the less dense RBC subpopulations. These results suggest that previously cryptic antigens were revealed by the activity of neuraminidase on the plasma membranes of the treated RBC.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 9
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    Isolation and characterization of an age-related antigen present on senescent human red blood cells (1981)
    American Society of Hematology
    Details
    Publication Date: 1981-08-01
    Description: Autologous membrane-bound IgG was isolated from a subpopulation of human red blood cells (RBC) with specific density greater than 1.110, by affinity chromatography of purified RBC membrane glycoprotein preparations using immobilized wheat germ agglutinin and immobilized anti-human immunoglobulin (Ig) as immunoabsorbents. The Ig-containing population thus obtained, when further separated by chromatography on Sephadex G-200 in the presence of chaotropic agents, yielded four peaks (Ia, Ib, II, and III). Double immunodiffusion revealed the presence of Ig in the first three peaks (IgM in peak Ia, IgA in Ib, and IgG in II) but not in peak III. Peak III was precipitated by the Ig-containing peaks (Ia, Ib, and II) in immunodiffusion assays, suggesting that the antigenic membrane determinants responsible for the binding of autologous Ig to senescent human RBC were contained in this peak (III). Peaks Ia, Ib and II precipitate purified asialoglycophorin; peak III was reactive with purified autoantibodies directed against asialoglycophorin. These results suggest that an age-related antigenic determinant(s) present on senescent human RBC is exposed by desialylation of the major sialoglycoprotein component of the RBC membrane.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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  • 10
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    Isolation and characterization of an age-related antigen present on senescent human red blood cells (1981)
    American Society of Hematology
    Details
    Publication Date: 1981-08-01
    Description: Autologous membrane-bound IgG was isolated from a subpopulation of human red blood cells (RBC) with specific density greater than 1.110, by affinity chromatography of purified RBC membrane glycoprotein preparations using immobilized wheat germ agglutinin and immobilized anti-human immunoglobulin (Ig) as immunoabsorbents. The Ig-containing population thus obtained, when further separated by chromatography on Sephadex G-200 in the presence of chaotropic agents, yielded four peaks (Ia, Ib, II, and III). Double immunodiffusion revealed the presence of Ig in the first three peaks (IgM in peak Ia, IgA in Ib, and IgG in II) but not in peak III. Peak III was precipitated by the Ig-containing peaks (Ia, Ib, and II) in immunodiffusion assays, suggesting that the antigenic membrane determinants responsible for the binding of autologous Ig to senescent human RBC were contained in this peak (III). Peaks Ia, Ib and II precipitate purified asialoglycophorin; peak III was reactive with purified autoantibodies directed against asialoglycophorin. These results suggest that an age-related antigenic determinant(s) present on senescent human RBC is exposed by desialylation of the major sialoglycoprotein component of the RBC membrane.
    Print ISSN: 0006-4971
    Electronic ISSN: 1528-0020
    Topics: Biology , Medicine
    Published by American Society of Hematology
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