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  • 1
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    Journal of periodontal research 22 (1987), S. 0 
    ISSN: 1600-0765
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The use of synchrotron X-ray diffraction has enabled us to record for the first time the first few orders of the collagen meridional low angle pattern from small, weakly diffracting native specimens of human periodontal ligament and gingival connective tissue, and to measure the D-period (fibrillar axis molecular overlap plus hole repeat) accurately. Comparison with human and other mammalian tendon and dermal specimens indicates that the D-period in both periodontal tissues resembles the value for dermal collagen, 65 nm, rather than that for tendon collagen, 67 nm.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Oxford, UK : Blackwell Publishing Ltd
    British journal of dermatology 102 (1980), S. 0 
    ISSN: 1365-2133
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The structure of the collagen fibres of the skin in the Ehlers-Danlos syndrome (ED-S) was studied in eight patients with ED-S Type I., three patients with ED-S Type II and three patients with the X-linked Type V.The results show that the reducible cross-links are present and undergo the same maturation process to non-reducible cross-links as in normal skin. Transmission electron microscopy revealed a normal ultrastructure of the collagen fibrils. At a higher morphological level of organization scanning electron microscopy demonstrated progressive increase in fibre bundle disorder from the X-linked to mitis, to gravis, in which the fibres making up the large fibre bundles demonstrated a considerable inability to aggregate.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-4838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Abstract Crystal preparations cleaned of organic deposits were extracted from cartilage deposits from osteoarthritic (OA) knee joints. These were studied by wide angle X-ray diffraction (WAXD) using a two-dimensional detector in order to ascertain the crystal species composition. Microcrystals in the mixtures were examined by scanning probe microscopy techniques to investigate the form and surfaces of individual particles. This examination resolved surface details on the crystals in the nanometre range. In some hydroxyapatite-rich deposits, small plate-like crystals closely resembling the intrafibrillar hydroxyapatite from calcifying turkey tendon collagen could be seen, suggesting these may have originally formed within collagen fibres. The surface features of triclinic calcium pyrophosphate dihydrate (T-CPPD), which were the predominant species of both synthetic crystals and CPPD from biological deposits, showed areas of relatively regular undulations of the order of 10 nm across and 3 nm deep. Their presence in synthetic crystals confirmed that this roughness, on the scale of a few unit cells, could not have arisen from the biological cleaning process. This suggested a mechanism whereby extra crystal surface could be made available for the location and adhesion of globular proteins, the majority of which tend to be of compatible molecular dimensions. This was tested by incubation of synthetic T-CPPD with human fibronectin, albumin and immunoglobulin G (IgG), followed by washing these free of unbound protein. Re-examination by SPM methods revealed arrays of the proteins located on the crystal surface and this confirmed the binding capacity of such crystals for proteinsin vivo.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Journal of materials science 5 (1994), S. 200-206 
    ISSN: 1573-4838
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Technology
    Notes: Vertebrate mineralized tissues are composite materials formed by the organized growth of carbonated apatite crystals within a matrix of collagen fibres. Calcified collagen from turkey tendon was investigated using scanning tunnelling microscopy (STM) and atomic force microscopy (AFM). Samples were treated with hydrogen peroxide to enhance the mineralized phase by removing part of the collagen matrix and the results compared with the untreated material. Plate-like crystalline entities with dimensions 35 nm × 5–8 nm by ∼ 1.5 nm were seen. These dimensions are consistent with previous reports using transmission electron microscopy (TEM) of calcified tendon and topographic imaging of tendon crystals. The resolution of the images obtained using STM is better than the previously reported pictures obtained using TEM or scanning electron microscopy (SEM). The value of 35 nm is the same as the gap region in the structure of the collagen fibrils. Stacking of plates and plate-aggregates are a dominant feature in the scanning images. These results support the concept of organized intra-fibril mineral crystals within the organic collagen matrix. Electron diffraction and X-ray diffraction were undertaken on the samples and the patterns recorded match those previously reported for carbonated apatite.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 33 (1993), S. 897-902 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Elongational flow techniques have been used to investigate the birefringent response of monodisperse type IV collagen in dilute solution and the results compared with type I. collagen. A four-roll mill apparatus was used to characterize the solutions at low strain rates, \documentclass{article}\pagestyle{empty}\begin{document}$\dot{\varepsilon}$\end{document} ≥ 300 s-1. The birefringence is nonlocalized and rises gradually to a plateau value, in accordance with rigid-rod behavior. The gradients of the tangent to the curves at zero strain rate are estimated for types IV and I collagen. The concentrations of the solutions used were in the dilute to semidilute regimes. Using a value of 300 nm for the length of type I collagen, values of 364-408 nm were calculated for the length of the type IV collagen molecule, depending on the concentration regime chosen, which is consistent with biochemical predictions based on a rigid molecule. The results imply that the behavior of type IV collagen molecules in solution is similar to type I collagen, despite the presence of several sequence interruptions in the type IV helix. © 1993 John Wiley & Sons, Inc.
    Additional Material: 5 Ill.
    Type of Medium: Electronic Resource
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