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  • 1
    Electronic Resource
    Electronic Resource
    Cationic Leukocyte Antigen in Urine of Patients with Chronic Myelocytic Leukaemia (1973)
    [s.l.] : Nature Publishing Group
    Nature 245 (1973), S. 379-380 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] We here report the presence of a second basic protein in leukaemic urine that does not cross react antigenically with human lysozyme. This cationic protein has a different electrophoretic mobility from lysozyme, RNase and DNase. Its molecular weight is 23,000 as determined by two-dimen sional SDS ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/245379a0
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  • 2
    Electronic Resource
    Electronic Resource
    Comparison of ribosomal RNA-binding protein “L2” isolated from different bacterial species (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 147-156 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A ribosomal protein (L“2”) which binds to 23S rRNA was isolated from 70S ribosomes of several Bacillacease. It was shown by two-dimensional gel electrophoresis, molecular weight determination, amino acid analysis and immunological methods that this protein is homologous to the E. coli ribosomal protein L2 which also binds to 23S rRNA. In all Bacillaceae this protein “L2” remains bound to 23S rRNA after extraction of ribosomal proteins with 4 M urea and 2 M LiCl, in contrast to E. coli. Immunological experiments demonstrated that the protein “L2” of B. stearothermophilus undergoes a conformational change when it binds to 23S RNA.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333662
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  • 3
    Electronic Resource
    Electronic Resource
    Determination of the location of proteins L14, L17, L18, L19, L22 and L23 on the surface of the 50S ribosomal subunit of Escherichia coli by immune electron microscopy (1974)
    Springer
    Molecular genetics and genomics 134 (1974), S. 187-208 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The location of the ribosomal proteins L14, L17, L18, L19, L22 and L23 on the surface of the 50S subunit of E. coli ribosomes was determined by immune electron microscopy. Antibodies (bivalent IgG's) specific for the six ribosomal proteins were used to form 50S subunit dimers (50S-IgG-50S). The dimers were separated from non-bound antibodies and 50S subunit-monomers and larger aggregates by sucrose density gradient centrifugation. The attachment of each of the six immunoglobulins to 50S subunits was visualized directly by electron microscopy using negative staining and correlated with one or more of the structural features of the particle. Each of the proteins was found to occupy a unique position. Proteins L14, L19 and L23 are located in the region of the 50S subunit which interacts with the 30S particle. Proteins L17 and L22 are on the opposite side of the 50S ribosomal subunit, whilst L18 holds a position on one of the lateral protuberances of a crown-like shaped 50S subunit. Two main forms of 50S subunits were seen on the electron micrographs: one of them had a crown-like shape; the second revealed kidney shaped images. It was demonstrated that these two images are only projections of one structure of the subunit that resembled an armchair; each of the forms could be transformed into the other through rotation by 90°. The results allowed the proposal of a three-dimensional model of the 50S subunit with the location of six different ribosomal proteins as illustrated in Fig. 13.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267715
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  • 4
    Electronic Resource
    Electronic Resource
    Location of proteins S5, S13 and S14 on the surface of the 30S ribosomal subunit from Escherichia coli as determined by immune electron microscopy (1974)
    Springer
    Molecular genetics and genomics 134 (1974), S. 209-223 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The structure of negatively stained 30 S ribosome-IgG-30 S ribosome complexes (“dimers”) was examined by electron microscopy to locate proteins S5, S13 and S14 on the surface of the 30S ribosomal subunit from Escherichia coli. The attachment points of non-crossreacting antibodies, specific to each of the three ribosomal proteins, were visualized and correlated to distinctive structural features of the 30S subunit. The 30S particle showed a bipartite structure of two globular sections unequal in size and connected by a narrow bridge (“neck”). Protein S5 was located at several sites on the surface of this neck region. Proteins S13 and S14 were localized in the smaller globular section and were found to be in close proximity to one another. A model of the 30 S subunit with the location of the three proteins is presented.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00267716
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  • 5
    Electronic Resource
    Electronic Resource
    Comparative immunological and electrophoretic studies on ribosomal proteins of Bacillaceae (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 129-145 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ribosomal proteins from several Bacillus species were compared by two-dimensional gel electrophoresis and immunological methods. The results revealed great heterogeneity among most Bacillus species. Comparison of ribosomal proteins from Bacilli with those of E. coli by two-dimensional gel electrophoresis showed little similarities, while structural homologies could be found by immunological methods. SDS two-dimensional gel electrophoresis revealed that the molecular weight of ribosomal proteins is conserved in all tested bacteria.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333661
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  • 6
    Electronic Resource
    Electronic Resource
    Immunological and electrophoretical comparison of ribosomal proteins from eight species belonging to Enterobacteriaceae (1973)
    Springer
    Molecular genetics and genomics 127 (1973), S. 111-128 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The ribosomal proteins of seven different Enterobacteriaceae were compared with those of E. coli by two-dimensional gel electrophoresis and by immunological methods. The ribosomal proteins of all Enterobacteriaceae were found to be very similar in molecular weight and in their electrophoretic properties. However, more dissimilarities could be detected by immunological methods thus indicating that few, if any, of the ribosomal proteins among the tested Enterobacteriaceae are identical. Ribosomes from all Enterobacteriaceae possess a protein which is electrophoretically identical with protein S7 from strain B (and not strain K) of E. coli.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00333660
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