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  • 1975-1979  (2)
  • 1960-1964  (2)
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  • 1
    Electronic Resource
    Electronic Resource
    Paralytic poliomyelitis in a child with agammaglobulinemia (1979)
    Springer
    European journal of pediatrics 132 (1979), S. 11-16 
    Details
    ISSN: 1432-1076
    Keywords: Poliomyelitis ; Agammaglobulinemia
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract This paper gives the clinical, immunological and virological data on a patient with agammaglobulinemia who developed paralytic poliomyelitis. The patient was a 3 year-old boy who had a typical B-cell defect without a T-cell defect. He had profound hypogammaglobulinemia and defective plasma cells and had repeated pyogenic infections which were controlled by gammaglobulin replacement therapy. At 3 years of age, he was admitted to our hospital with suspected meningitis. He had fever, tremor and neck stiffness for 3 days and subsequently developed paralysis in his left arm and right leg. There was lymphocytosis in the cerebrospinal fluid. A non vaccine-like strain of poliovirus type 2 was isolated from the stool.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00443199
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Preparation of Crystalline Pseudomonas cytochrome Oxidase and Some of its Properties (1962)
    [s.l.] : Nature Publishing Group
    Nature 194 (1962), S. 759-760 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] FROM the anaerobically cultivated cells of Pseudo-monas aeruginosa, a cytochrome which has all the properties of a cytochrome oxidase has been purified in an ultracentrifugally homogeneous state, and it was named Pseudomonas (P.) cytochrome oxidase1'2. The P. cytochrome oxidase has two hsems, hsem ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/194759a0
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    Paper (German National Licenses)
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  • 3
    Electronic Resource
    Electronic Resource
    DISTRIBUTION AND OPTICAL ACTIVITY OF THE BASIC PROTEIN IN BOVINE PERIPHERAL NERVE MYELIN (1977)
    Oxford, UK : Blackwell Publishing Ltd
    Journal of neurochemistry 29 (1977), S. 0 
    Details
    ISSN: 1471-4159
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Abstract— Antiserum to BF protein isolated from bovine spinal roots has been used to study the distribution of the protein in other species and tissues.Significant amounts of protein could be demonstrated in bovine, pig and rabbit peripheral nerve myelin. It was, however, scarcely detectable in guinea pig peripheral nerve myelin. There was BF protein in rabbit spinal cord as well as in peripheral nerve, but little or no BF protein in the liver, kidney, muscle or brain. BF protein in bovine spinal cord was localized in the myelin. The ratio of the BF protein to the encephalitogenic protein in the spinal cord myelin was around 0.15:1.0. BF protein was extractable from peripheral nerve myelin by saline as well as by acid solutions.The circular dichroism spectrum of the BF protein in aqueous solution suggested that this protein contained a very large amount of β-structure. This structure was not considered to be the result of acid denaturation because the protein purified from the saline extract of peripheral nerve also showed a similar spectrum.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1111/j.1471-4159.1977.tb03924.x
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    Paper (German National Licenses)
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  • 4
    Electronic Resource
    Electronic Resource
    Identity of Pseudomonas Cytochrome Oxidase with Pseudomonas Nitrite Redcutase (1964)
    [s.l.] : Nature Publishing Group
    Nature 204 (1964), S. 253-255 
    Details
    ISSN: 1476-4687
    Source: Nature Archives 1869 - 2009
    Topics: Biology , Chemistry and Pharmacology , Medicine , Natural Sciences in General , Physics
    Notes: [Auszug] IT is well known that, in the living cell, oytochromo oxidase catalyses the reaction of molecular oxygen with electrons liberated from various substrates. In most animal tissues, in many plant tissues and in some microorganisms, cytochromo a is known to function as the cytochrome oxidase1. On the ...
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1038/204253a0
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    Paper (German National Licenses)
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