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  • 1965-1969  (13)
Source
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Biochemistry of Viruses (1966)
    Palo Alto, Calif. : Annual Reviews
    Annual Review of Biochemistry 35 (1966), S. 299-334 
    Details
    ISSN: 0066-4154
    Source: Annual Reviews Electronic Back Volume Collection 1932-2001ff
    Topics: Chemistry and Pharmacology , Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1146/annurev.bi.35.070166.001503
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Buchbesprechungen (1966)
    Springer
    Naturwissenschaften 53 (1966), S. 92-92 
    Details
    ISSN: 1432-1904
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology , Natural Sciences in General
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00594779
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    Untersuchungen am Odontoglossum ringspot Virus, einem Verwandten des Tabakmosaik-Virus (1965)
    Springer
    Molecular genetics and genomics 97 (1965), S. 186-203 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00897495
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Lokalisierung von Aminosäureaustauschen bei Nitritmutanten des Tabakmosaikvirus (1965)
    Springer
    Molecular genetics and genomics 97 (1965), S. 305-326 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The positions of amino acid exchanges within eleven mutants of tobacco mosaic virus (TMV) isolated after treatment with nitrous acid have been localized. The protein chemical results are given in Tables 1–11 in detail and summarized in Table 12. In the discussion the localized amino acid exchanges of 36 mutants which arose spontaneously or were isolated after nitrite treatment or fluorouracil incorporation and whose primary protein structure have been described in this and earlier papers were compared with the current “codon dictionary”. All of the amino acid exchanges can be “explained” by the postulation that alteration of only one of the three nucleotides within a codon (Table 13) has occurred. Of the 26 amino acid exchanges localized in mutants isolated after treatment with nitrous acid all but two (isoleucin→methionine and glutamic acid→aspartic acid) are compatible with the nucleotide alterations C→U and A→G postulated for the action of nitrous acid on TMV-RNA. The distribution of the localized amino acid exchanges along the protein chain of TMV is shown in Fig. 1.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02035935
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  • 5
    Electronic Resource
    Electronic Resource
    Coat proteins of strains of two RNA viruses: Comparison of their amino acid sequences (1967)
    Springer
    Molecular genetics and genomics 100 (1967), S. 358-363 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The amino acid sequences of four strains of tobacco mosaic virus isolated in different parts of the world are compared. The differences between the strains are discussed with respect to special proteinchemical features (such as beginning of the chain, deletion of amino acids, number of different amino acids, sizes and distribution of regions with invariable amino acids) and with respect to the possibility of deducing the most probable nucleotide sequence for the coat protein cistron of tobacco mosaic virus. The complete amino acid sequences of the two RNA bacteriophage strains fr and f2 are compared. According to their coat proteins three groups of phages can be formed: 1) MS 2, f2 M 12 and R 17, 2) fr and 3) Qβ.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334062
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    Paper (German National Licenses)
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  • 6
    Electronic Resource
    Electronic Resource
    Ribosomal proteins (1968)
    Springer
    Molecular genetics and genomics 101 (1968), S. 70-81 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Ribosomal proteins of E. coli and yeast were separated by gel filtration on dextran (Sephadex) and polyacrylamide (Bio-Gel) columns. Both gels revealed a valuable separation of the proteins. Finally only Bio-Gel columns were used, since their polyacrylamide matrix is more resistant to the applied organic acids. The wide distribution of the molecular weights for both the E. coli and yeast ribosomal proteins was confirmed. E. coli ribosomal proteins were separated into three main groups by a single chromatography on Bio-Gel P-10. The same was true for yeast ribosomal proteins. Rechromatography of these protein groups resulted in a further valuable resolution. The fractionated proteins are recovered without any loss and they are very useful for further purification by other procedures, especially on a large scale basis.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00434813
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  • 7
    Electronic Resource
    Electronic Resource
    Ribosomal proteins (1967)
    Springer
    Molecular genetics and genomics 100 (1967), S. 364-373 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The proteins of E. coli ribosomes were separated by a specially developed type of preparative polyacrylamide gel electrophoresis and proteins corresponding to 16 of the separated bands have so far been isolated. The amino acid compositions and the tryptic peptide maps of these proteins show certain degree of similarity as well as distinct differences. Determination of molecular weights revealed a wide range: The lowest molecular weight was 9,000 and the highest 41,000 for the proteins so far studied. The similarities between various ribosomal proteins in their amino acid compositions and their peptide maps on one hand and the wide range in their molecular weights on the other hand can be explained by a hypothesis involving gene duplications.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00334063
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  • 8
    Electronic Resource
    Electronic Resource
    Ribosomal proteins (1968)
    Springer
    Molecular genetics and genomics 103 (1968), S. 238-243 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary A comparison of the protein patterns of the 70S and 80S ribosomes from various plants, E. coli and yeast by disc-gel electrophoresis has shown the following relations: 1. There is a greater similarity between chloroplast ribosomes from various plants than between chloroplast and cytoplasmic ribosomes obtained from the same plant. 2. The protein patterns of the cytoplasmic ribosomes from bean, spinach and tobacco are more similar to each other than when compared to that of wheat germ. 3. At least one band is common to cytoplasmic ribosomes from all plants tested. 4. Only very few bands with identical mobilities are observed between chloroplast and E. coli ribosomes and between cytoplasmic plant and yeast ribosomes.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00273693
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  • 9
    Electronic Resource
    Electronic Resource
    Ribosomal proteins (1968)
    Springer
    Molecular genetics and genomics 101 (1968), S. 82-88 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Proteins from yeast ribosomes were separated by preparative polyacrylamide electrophoresis. The amino acid compositions, peptide maps and molecular weights of the various isolated proteins were determined and compared. Similarities in amino acid compositions between a) the various proteins of yeast ribosomes and b) the ribosomal proteins of yeast and E. coli are discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00434814
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  • 10
    Electronic Resource
    Electronic Resource
    Über die Frage der Mehrdeutigkeit des genetischen Codes, untersucht am Hüllenprotein des Tabakmosaikvirus (1965)
    Springer
    Molecular genetics and genomics 97 (1965), S. 138-149 
    Details
    ISSN: 1617-4623
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary An investigation has been made of whether ambiguity of the genetic code, i.e. variation in the translation of the genetic message produced by some external factors, occurs in tobacco plants infected with tobacco mosaic virus (TMV). This effect ist known to occur in bacterial systems. The following experiments have been done: a) TMV-vulgare infected plants were kept at five different temperatures between the minimum (12°C) and maximum (37°C) of the virus multiplication. b) TMV-A14 was grown in leaves in the presence of high concentrations of each of the following three cations: streptomycin, spermine, Mg++. c) Plants infected with the TMV mutant Ni 1927 were kept under the same conditions as in and b. After isolation of the virus the following proteinchemical methods were applied to the virus preparations which were grown under the eight conditions mentioned above: a) Amino acid analyses of the whole coat protein of TMV vulgare, b) separation of the RNA from the coat protein of vulgare and A 14, digestion of the proteins with trypsin, isolation of all tryptic peptides by column and paper chromatography, hydrolysis and analysis of the amino acid composition of each peptide, c) quantitative determinations of the terminal amino acids split off by treatment of Ni 1927 with carboxypeptidase A. The analyses of all virus preparations gave the same results: within the experimental errors (1–2% and 5% depending on the method) there is no variation in the amino acid compositions of the tryptic peptides as a consequence of the various polycations or temperatures. The same result has been found with X-protein isolated from leaves in which the virus was synthesized in the presence of streptomycin. From the foregoing analyses it was concluded that translation of the genetic information into the amino acid sequence of TMV protein is influenced, if at all, to such a low extent that this effect cannot be found by the current methods of proteinchemistry.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00897491
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