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  • 1980-1984  (2)
  • 1
    Online Resource
    Online Resource
    Institute of Organic Chemistry & Biochemistry ; 1982
    In:  Collection of Czechoslovak Chemical Communications Vol. 47, No. 9 ( 1982), p. 2403-2414
    In: Collection of Czechoslovak Chemical Communications, Institute of Organic Chemistry & Biochemistry, Vol. 47, No. 9 ( 1982), p. 2403-2414
    Abstract: The title compound crystallizes in the monoclinic system, has the P 2 1 / c space group, and the unit cell parameters are a = 1 484.4(8), b = 1 522.8(8), c = 1 854.0(8) pm, β = 96.36(4)°, Z = 4. The structure consists of molecules of an electroneutral complex interconnected only through the van der Waals forces. Solvent is nonstoichiometrically incorporated in the crystals. Octanolactam monodentate ligands are coordinated through oxygen atoms to Cr(III) and have the cis -conformation of the amide group. The relationship between structure parameters of the amide group, their change caused by coordination and the reactivity of the amide group to nucleophilic substitution are discussed using the example of octanolactam polymerization.
    Type of Medium: Online Resource
    ISSN: 0010-0765 , 1212-6950
    Language: English
    Publisher: Institute of Organic Chemistry & Biochemistry
    Publication Date: 1982
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  • 2
    Online Resource
    Online Resource
    The Company of Biologists ; 1984
    In:  Journal of Cell Science Vol. 69, No. 1 ( 1984-07-01), p. 47-65
    In: Journal of Cell Science, The Company of Biologists, Vol. 69, No. 1 ( 1984-07-01), p. 47-65
    Abstract: Septum-defective mutants of Schizosaccharomyces pombe impaired in cdc genes 3, 4, 8 and 12 were compared by fluorescence microscopy, freeze-etching and ultrathin sectioning. This approach made it possible to recognize the internal organization of defective phenotypes under restrictive conditions. Of special interest in this study was the pattern of unusual septum malformations found to be regular features of the terminal phenotypes of the mutants. Their overall topology was visualized at the cellular level by primulin fluorescence. The subcellular location of septum defects was found to be identical in origin to the compartment where normal septum was assembled in the wild type. Delocalized septation involved both microfibrillar and matrix components, which participated in the final assembly of malformations. Unique contour views of delocalized septa were exposed by freeze-fracturing. Cytoplasmic microtubules and microfilaments were detected in ultrathin sections of the cytoplasm of mutant cells. The internal organization of malformationaccumulating phenotypes suggested a disruption of the directional mechanism that steers septum material to the periplasm at the cell equator.
    Type of Medium: Online Resource
    ISSN: 0021-9533 , 1477-9137
    Language: English
    Publisher: The Company of Biologists
    Publication Date: 1984
    detail.hit.zdb_id: 219171-4
    detail.hit.zdb_id: 1483099-1
    SSG: 12
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