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  • 1
    Electronic Resource
    Electronic Resource
    STUDIES OF AN UNUSUAL BICLONAL GAMMOPATHY: IMPLICATIONS WITH REGARD TO GENETIC CONTROL OF NORMAL IMMUNOGLOBULIN SYNTHESIS (1971)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 190 (1971), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1971.tb13559.x
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  • 2
    Electronic Resource
    Electronic Resource
    Combustion Synthesis and Characterization of Nanocrystalline Tin and Tin Oxide (SnOx, x= 0–2) Particles (2004)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of the American Ceramic Society 87 (2004), S. 0 
    Details
    ISSN: 1551-2916
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Nanocrystalline SnOx particles (x= 0–2) were synthesized using tetramethyltin (Sn(CH3)4) vapor as the particle precursor reactant in hydrogen/oxygen/argon (H2/O2/Ar) flames. The particle composition and morphology were characterized using X-ray diffractometry, transmission electron microscopy, and nitrogen (N2) surface adsorption. By controlling the concentration of oxygen in the reactant gases and the flame temperatures, metallic tin (Sn), tin monoxide (romarchite SnO), and/or tin dioxide (cassiterite SnO2) were generated. The crystalline powders consisted of both discrete primary particles and agglomerates, with average primary particle sizes of 23–24 nm for SnO2 and 69 nm for Sn (based on specific surface area measurements of bulk powders collected in the exhaust region of the flame). The compositional results were interpreted using equilibrium and detailed chemical kinetics models.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1151-2916.2004.tb06356.x
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  • 3
    Electronic Resource
    Electronic Resource
    Biochemical and Immunologic Comparisons of Three Forms of Thy-1 Molecules Isolated from Human Brains (1987)
    Oxford, UK : Blackwell Publishing Ltd
    Annals of the New York Academy of Sciences 496 (1987), S. 0 
    Details
    ISSN: 1749-6632
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1749-6632.1987.tb35783.x
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  • 4
    Electronic Resource
    Electronic Resource
    A MARMOSET T-LYMPHOCYTE PROTEIN RELATED TO DEFINED HUMAN SERUM IMMUNOGLOBULIN AND FRAGMENTS (1981)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 8 (1981), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: Current concepts of the antigen-specific receptor of thymus-derived (T) lymphocytes suggest that this molecule bears immunoglobulin (Ig) variable (V) regions, but does not represent a classical serum antibody. We immunized rabbits with a globulin fraction obtained from an in vitro cultured marmoset T cell lymphoma line which expressed surface components related to immunoglobulins. Quantitative immunoprecipitation and competition radioimmunoassay studies carried out using characterized monoclonal human Igs and their chains and fragments show that this rabbit antiserum, raised aginst a T cell product, reacts with a particular, conformational VH-determinant which is formed by interaction with λ light chains and with two μ chain (IgM) related determinants. Neither μ chain determinant is a major isotype specific marker, and each occurs only on certain distinct subsets of serum μ chains. One is located in the Fc fragment; the location of the other μ related determinant is not known. These results show that this rabbit antiserum recognizes both variable and constant region determinants on the T cell receptor heavy chain. Rabbit antibody to the T cell product which cross-reacts with serum μ chain was isolated by immune affinity chromatography on Sepharose-derivatized covalently with one particular reactive IgM protein, the Waldenstrom macroglobulin Can (kμ). This antibody precipitated a biosynthetically-labelled component of approximate M. W. 70,000 as assessed by polyacrylamide gel electrophoresis in Na Dod SO4-containing buffers. These data support the conclusion that certain T cells express and synthesize a molecule related to Ig VH-regions which also has a constant region sharing antigenic markers with IgM subpopulations.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1981.tb00754.x
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  • 5
    Electronic Resource
    Electronic Resource
    IMMUNOGLOBULIN EVOLUTION: CHEMICAL STUDY OF CLAWED TOAD (XENOPUS LAEVIS) HEAVY AND LIGHT CHAINS (1978)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 5 (1978), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: NH2, terminal amino acid sequence determinations of clawed toad (Xenopus laevis) immunoglobulins indicate that approximately 30% of the heavy chains and less than 5% of the light chains have unblocked NH2 termini. The major amino acid sequence of the X. laevis 7S immunoglobulin heavy chains is the same as that of the 19S immunoglobulin heavy chains. Thus in the synthesis of the heavy chains, the VH genes coding for unblocked heavy chains can associate with CH genes of both the 19S and 7S classes. This association is particularly important in amphibians because, in contrast to mammals and birds, the majority of amphibian antibody-producing cells synthesize both 19S and 7S immunoglobulins and do not participate in the ‘genetic switch’ characteristic of lymphocyte differentiation in higher organisms. In X. laevis, the major amino acid sequence at the first twenty-four positions of the unblocked heavy chains shows approximately 54% difference from the prototype amino acid sequence of the mammalian VHIII subgroup. Thus, the VHIII gene(s) must have started to appear after the evolutionary divergence of the common ancestor of mammals and birds from the amphibian line. The amino acid composition of the X. laevis 7S immunoglobulin heavy chains differs from that of its 19S immunoglobulins as well as those of human IgG and IgA. These data support the concepts (a) that amphibian 7S and 19S immunoglobins belong to distinct classes and (b) that amphibian 7S immunoglobulin does not resemble mammalian IgG or IgA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1978.tb00665.x
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  • 6
    Electronic Resource
    Electronic Resource
    BIOCHEMICAL CHARACTERIZATION OF HUMAN THY-1 (1984)
    Oxford, UK : Blackwell Publishing Ltd
    International journal of immunogenetics 11 (1984), S. 0 
    Details
    ISSN: 1744-313X
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Biology , Medicine
    Notes: The human Thy-1 homologue (p25) was characterized biochemically for amino acid composition, sequence and carbohydrate content. Two other forms of the human Thy-1 molecule were detected and partially characterized. A 40,000 mol.wt. molecule (p40) is the dimer of p25 and its formation is increased by the presence of sodium dodecyl sulphate (SDS). The second form of 16,000 mol.wt. (p16) appears to be a cryptic or breakdown form of p25. Comparison of the amino acid compositions of p25, p40 and p16 isolated from MOLT-3 cells, with that deduced from the nucleotide sequence of the gene coding for part of the putative T cell antigen receptor, also from MOLT-3 cells, shows that the Thy-1 homologue is distinct from, but evolutionary related to, one of the putative T cell antigen receptor polypeptide chains.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1744-313X.1984.tb00815.x
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