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  • 1
    Electronic Resource
    Electronic Resource
    s.l. : American Chemical Society
    Biochemistry 30 (1991), S. 2827-2833 
    ISSN: 1520-4995
    Source: ACS Legacy Archives
    Topics: Biology , Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 2
    ISSN: 1573-4935
    Keywords: Semliki Forest virus (SFV) ; virus entry ; nucleocapsid disassembly ; capsid protein
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Chemistry and Pharmacology
    Notes: Abstract Semliki Forest virus (SFV) envelope proteins function as proton pores under mildly acidic conditions and translocate protons across the viral membrane [Schlegel, A., Omar, A., Jentsch, P., Morell, A. and Kemp, F. C. (1991) Biosci. Rep. 11, 243–255]. As a consequence, during uptake of SFV by cells via receptor-mediated endocytosis the nucleocapsid is supposed to be exposed to protons. In this paper the effects of mildly acidic pH on SFV nucleocapsids were examined. A partial proteolytic fragmentation of core proteins was observed when nucleocapsids were exposed to mildly acidic pH. A similar proteolytic event was detected when intact SFV virions were exposed to identical conditions. Protease protection assays with exogenous bromelain provided evidence that the capsid protein degradation was due to an endogenous proteolytic activity and not to a proteolytic contamination. Detergent solubilization of virus particles containing degraded nucleocapsids followed by sucrose gradient centrifugation led to a separation of capsid protein fragments and remaining nucleocapsids. These data are discussed in terms of a putative biological significance, namely that the core protein fragmentation may play a role in nucleocapsid disassembly.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    The protein journal 11 (1992), S. 388-389 
    ISSN: 1573-4943
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Die Makromolekulare Chemie 179 (1978), S. 677-695 
    ISSN: 0025-116X
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Physics
    Notes: Liquid phase pairs were found in which polystyrene (PS) and styrene-acrylonitrile (SAN)-copolymers with an AN-content up to 13 wt.-% can be partitioned. They could be used for the fractionation of the copolymers according to chemical composition. The phase pairs are composed of 4 solvents, cyclohexane and nitromethane to form the phases and two solvents for the polymers. The partition ratio was measured as a function of the composition of the phase pairs, the molecular weight of PS, and of the AN-content of the copolymers. The phase composition at which a polymer is equally distributed into both phases depends on the chemical composition of the polymer but not on its molecular weight. With other phase compositions the partition equilibrium is shifted to one phase or the other the more the degree of polymerisation increases. Based on the partition equilibrium, fractionation methods are proposed to separate the SAN-copolymers according to their chemical composition if their molecular weight is high enough (〉about 105). The conditions which determine fractionation more by molecular weight or more by chemical composition are discussed.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
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  • 5
    ISSN: 1432-1955
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Four variants and/or posttranslational modifications of histone H1-like proteins ofTrypanosoma brucei brucei procyclic culture forms were extracted with 0.25N HCl from isolated nuclei and analyzed by two-dimensional gel electrophoresis. The amino acid composition of these proteins, their ability to space nucleosomes regularly and to induce salt-dependent condensation of the chromatin indicated their histone H1 nature. On the other hand, the histone H1-like proteins clearly differed from their higher-eukaryote counterparts by their weak interaction with DNA under low-salt conditions. As a consequence, intact nucleosome filaments were prepared according to a new preparation protocol especially adapted to the unstable chromatin ofT. b. brucei. Our results indicate that the biochemical properties of the histone H1-like proteins contribute to the structural and functional differences between the chromatin of procyclicT. b. brucei and that of higher eukaryotes.
    Type of Medium: Electronic Resource
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  • 6
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Journal of Applied Polymer Science 25 (1980), S. 783-794 
    ISSN: 0021-8995
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Graft copolymerization of acrylonitrile onto a soluble wool keratin derivative was studied with the reduced and carboxymethylated low-sulfur protein fraction from wool. Copolymerization was carried out under a variety of conditions with a redox system of (NH4)2S2O8-Na2SO3 in 60% (w/w) aqueous ZnCl2 solution at 10°C. Monomer conversions higher than 90% were obtained by the stepwise addition of initiator. The graft products were successfully separated into grafted copolymer and homopolyacrylonitrile (PAN) by fractional precipitation or solvent extraction with DMF. Grafted PAN were isolated by acid hydrolysis of the keratin backbone. Characterization of grafted and homo-PAN was carried out by IR spectroscopy, amino acid endgroup analysis, and viscometry. On the basis of the results, effects of polymerization conditions on grafting parameters were discussed. Membranes were prepared from 60% aqueous ZnCl2 solution by using ice-cold water as the regenerating medium. All the membranes formed from the graft products were transparent. Observation by scanning electron microscopy showed that the surface consisted of rather spherical keratin domains regularly distributed in the PAN matrix. Selective hydrolysis of the keratin domains allowed a new type of porous PAN membrane to be obtained, with the inner walls of the pores being charged with amino acid residues attached to PAN chains as the endgroup.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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