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  • 1985-1989  (4)
  • 1975-1979  (1)
  • 1970-1974
  • 1950-1954
  • 1925-1929
  • 1915-1919
  • 1910-1914
  • Proteoglycans  (3)
  • 07.77  (1)
  • 58G11  (1)
Material
Years
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Applied physics 43 (1987), S. 247-255 
    ISSN: 1432-0630
    Keywords: 78.70BJ ; 07.77
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics , Physics
    Notes: Abstract Low-energy intense positron beams derived from pair production can be made at high-energy electron linacs and such beams are in operation or under installation at several linac facilities. Using a pulsed position beam made at a 100 MeV electron linac, we have measured the intensity and velocity distribution of positronium emitted from materials by measuring the time-of-flight of annihilating positronium. The time-of-flight data are augmented by positron lifetime and angular correlation measurements performed with the beam. Positronium spectra have been measured for a number of metallic samples. Several new observations have been made including details of the energy distribution of positronium emission formed by a thermalized positron and a conduction electron and the production of positronium from energetic positrons scattered out of the sample.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 27 (1979), S. 75-82 
    ISSN: 1432-0827
    Keywords: Proteoglycans ; Hydroxyapatite ; Amorphous calcium phosphate ; Nucleation ; Calcification
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary Well-characterized bovine nasal proteoglycan A1 fraction (aggregate) and proteoglycan D1 fraction (subunit) have been shown to be effective inhibitors of hydroxyapatite (HA) formation in two in vitro test systems: (a) the transformation of amorphous calcium phosphate (ACP) to crystalline HA, and, (b) the direct precipitation of HA from low-concentration calcium phosphate solutions. A1 or D1 in solution slowed the transformation kinetics in system (a) without affecting the time to the onset of conversion. In system (b), A1 or D1 in solution increased the time to the onset of HA formation without affecting the HA formation kinetics. In both test systems A1 was a more effective inhibitor than D1, although the difference was not great. In both systems the inhibitory effect was proportional to the A1 or D1 solution concentration. The action of solutions of low and high molecular weight neutral dextrans on both test systems showed that high molecular weight and/or extended spatial molecular conformation has a much stronger correlation with inhibitory ability than solution viscosity. Proteoglycans have been implicated as playing a role in regulating biological mineralization particularly in the epiphyseal growth plate. Our study suggests that just enzymatic cleavage of aggregate into subunit is not sufficient to allow mineralization to occur, since we find that D1 itself is a potent inhibitor of HA formation. Further degradation and/or removal of D1 appears to be necessary for calcification to take place.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Acta applicandae mathematicae 12 (1988), S. 1-33 
    ISSN: 1572-9036
    Keywords: 58G11 ; 58G32 ; 60H15 ; Bochner's theorem ; Brownian motion and heat flow ; spectrum of the Laplacian ; hyperbolic manifolds ; cohomology with compact support
    Source: Springer Online Journal Archives 1860-2000
    Topics: Mathematics
    Notes: Abstract Bochner's theorem that a compact Riemannian manifold with positive Ricci curvature has vanishing first cohomology group has various extensions to complete noncompact manifolds with Ricci possibly negative. One still has a vanishing theorem for L 2 harmonic one-forms if the infimum of the spectrum of the Laplacian on functions is greater than minus the infimum of the Ricci curvature. This result and its analogues for p-forms yield vanishing results for certain infinite volume hyperbolic manifolds. This spectral condition also imposes topological restrictions on the ends of the manifold. More refined results are obtained by taking a certain Brownian motion average of the Ricci curvature; if this average is positive, one has a vanishing theorem for the first cohomology group with compact supports on the universal cover of a compact manifold. There are corresponding results for L 2 harmonic spinors on spin manifolds.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Hoboken, NJ [u.a.] : Wiley-Blackwell
    Journal of Orthopaedic Research 7 (1989), S. 146-151 
    ISSN: 0736-0266
    Keywords: Intervertebral disc ; Cartilage ; Proteoglycans ; Electron microscopy ; Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: Articular cartilage and the intervertebral disc tissues have different material and biological properties and different patterns of aging and degeneration. To determine if the proteoglycans of these tissues differ in structure, we used the electron microscopic monolayer technique to compare baboon articular cartilage proteoglycans with baboon annulus fibrosus, transition zone, and nucleus pulposus proteoglycans. Intervertebral disc and articular cartilage porteoglycans differed signficantly. Articular cartilage contained large proteoglycan aggregates formed from hyaluronic acid central filaments, multiple monomers, and large nonaggregated monomers. These molecules were identical to those of nasal cartilage, growth plate cartilage, chondrosarcomas, or menisci. In contrast, the intervertebral disc tissues contained only nonaggregated proteoglycan monomers and clusters of monomers without apparent central filaments. Intervertebral disc nonaggregated monomers were shorter and more variable in length than those from articular cartilage, and nucleus pulposus nonaggregated monomers were even shorter and more variable in length than transition zone and annulus fibrosus monomers. These observations suggest that significant differences in proteoglycan metabolism exist between articular cartilage and intervertebral disc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    Hoboken, NJ [u.a.] : Wiley-Blackwell
    Journal of Orthopaedic Research 4 (1986), S. 1-9 
    ISSN: 0736-0266
    Keywords: Proteoglycans ; Growth plate ; Mineralization ; Electron microscopy ; Life and Medical Sciences
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Medicine
    Notes: To investigate possible structural changes in reassembled proteoglycan aggregates during cartilage mineralization, we examined the molecular architecture and dimensions of growth plate proteoglycan aggregates by electron microscopy. The ends of fetal bovine femurs and tibias were separated into three regions: the epiphysis; the cartilage growth plate, consisting of the proliferative zone and the unmineralized portion of the hypertrophic zone; and the calcified portion of the hypertrophic zone along with part of the metaphysis. Aggregates from all three regions had the same molecular architecture. They consisted of central hyaluronic filaments with multiple attached monomers. Monomers consisted of two segments: (a) a peripheral thick segment, which represents primarily the chondroitin sulfate-rich region, and (b) a thin segment attached directly to the hyaluronic acid filament. The length of aggregated monomers did not differ between the growth plate cartilage and the metaphysis, nor did the lengths of the thin and thick segments, indicating that the chondroitin sulfate-rich region of aggregated monomers is not degraded during cartilage mineralization. Between the growth plate cartilage and the metaphysis, aggregates became shorter and had fewer monomers and wider spacing between monomers. These structural alterations in proteoglycan aggregates may be one of the events that prepares the matrix for mineralization.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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