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  • Organic Chemistry  (2)
  • /  (1)
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  • 1
    Electronic Resource
    Electronic Resource
    Calcium-binding proteins in the retina of a calbindin-null mutant mouse (1998)
    Springer
    Cell & tissue research 292 (1998), S. 211-218 
    Details
    ISSN: 1432-0878
    Keywords: Key words Calbindin ; Parvalbumin ; Calretinin ; Neurofilament protein ; Calmodulin-like protein ; Mouse [calbindin null mutant ( ; / ; )]
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract  Calcium-binding proteins are abundantly expressed in many neurons of mammalian retinae. Their physiological roles are, however, largely unknown. This is particularly true for calcium-modulating proteins (“calcium buffers”) such as calbindin D28k. Here, we have studied retinae of wildtype (+/+) and calbindin-null mutant (–/–) mice by using immunocytochemical methods. Although calbindin immunoreactivity was completely absent in the calbindin (–/–) retinae, those cells that express the protein in wildtype retinae, such as horizontal cells, were still present and appeared normal. This was verified by immunostaining horizontal cells for various neurofilament proteins. In order to assess whether other calcium-binding proteins are upregulated in the mutant mouse and may thus compensate for the loss of calbindin, mouse retinae were also immunolabeled for parvalbumin, calretinin, and a calmodulin-like protein (CALP). In no instance could a change in the expression pattern of these proteins be detected by immunocytochemical methods. Thus, our results show that calbindin is not required for the maintenance of the light-microscopic structure of the differentiated retina and suggest roles for this protein in retinal function.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/s004410051052
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Stoffwechselprodukte von Mikroorganismen. 231. Mitteilung230. Mitteilung s. [1].. Bafilomycin-A1-21-O-(α-L-rhamnopyranosid): Strukturaufklärung durch chemische Verknüpfung mit Bafilomycin A1 und Leucanicidin (1985)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 68 (1985), S. 83-94 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Isolation of Bafilomycin-A1-21-O-(α-L-rhamnopyranoside). Structural Determination by Chemical Correlation with Bafilomycin A1 and LeucanicidinFrom cultures of an actinomycete strain, the known antifungal and insecticidal antibiotic leucanicidin (1) and a hitherto unknown antifungal antibiotic, bafilomycin-A1-21-O-(α-L-rhamnopyranoside) (2), were isolated. The latter is spectroscopically closely related to 1 and bafilomycin A1 (3) and gave degradation products identical with compounds obtained by analogous degradation of 1 and 3.
    Additional Material: 5 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19850680111
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  • 3
    Electronic Resource
    Electronic Resource
    Stoffwechselprodukte von Mikroorganismen. 236. Mitteilung235. Mitteilung: [1]. Schwefelhaltige Ansa-Verbindungen des Naphthomycin-Typus (1986)
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 69 (1986), S. 1356-1364 
    Details
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Metabolites of Microorganisms. Sulfur-Containing Ansa Compounds of the Naphthomycin TypeFrom a strain of Streptomyces (Tü 2357) in addition to naphthomycin A, 4 new yellow pigments were isolated and their structures determined by spectroscopic comparison with naphthomycin A. Whereas the naphthomycins D and E are simple derivatives of naphthomycin A, having OH and H, respectively, instead of Cl, the naphthomycins F and G contain an N-acetylcysteine residue linked to the aromatic moiety by a thioether group. Degradations with O3 yielded identical products from the naphthomycins A, D, F, and G, showing coincident configurations in parts of the molecules. Naphthomycin F shows some biological activity against gram-positive bacteria and fungi, although much weaker than naphthomycin A. The naphthomycins D, E, and G are inactive against microorganisms.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/hlca.19860690610
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