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  • 1
    Electronic Resource
    Electronic Resource
    Conformational changes in human prothrombin as detected by antibody populations
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Protein Structure and Molecular 996 (1989), S. 95-102 
    Details
    ISSN: 0167-4838
    Keywords: (Human) ; Calcium ; Conformational change ; Prothrombin fragment 1
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0167-4838(89)90100-3
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  • 2
    Electronic Resource
    Electronic Resource
    The induction of large unilamellar vesicle fusion by cationic polypeptides: the effects of mannitol, size, charge density and hydrophobicity of the cationic polypeptides
    Amsterdam : Elsevier
    Biochimica et Biophysica Acta (BBA)/Biomembranes 860 (1986), S. 314-324 
    Details
    ISSN: 0005-2736
    Keywords: Calcium ; Cationic polypeptide ; Charge density ; Mannitol ; Membrane fusion ; Polylysine
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Medicine , Physics
    Type of Medium: Electronic Resource
    URL: http://linkinghub.elsevier.com/retrieve/pii/0005-2736(86)90528-6
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  • 3
    Electronic Resource
    Electronic Resource
    Rhythmic dentinogenesis in the rabbit incisor: Allometric aspects (1980)
    Springer
    Calcified tissue international 32 (1980), S. 45-53 
    Details
    ISSN: 1432-0827
    Keywords: Dentin ; Periodicity ; Allometry ; Calcium ; Sulfur
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary We have described differences in the aspects of biological rhythms for calcium and sulfur deposition on the labial and lingual sides of the growing rabbit incisor, where growth occurs along a spiral axis. The calcium oscillations appear to be smoother on the labial side than on the lingual side. The lingual side is characterized by high-frequency rhythms with high amplitudes which possess the greatest percent of the power (Fourier analysis). These observations also reflect a difference in behavior of the mean Ca concentration across the labial and lingual sides. Sulfur rhythms on the labial side have higher amplitudes than those on the lingual side, but systematic differences in distribution of power between high and low frequencies is not as pronounced as in the case of Ca. The differences in Ca rhythms reflect differences in the growth rates of incisors on either side of the spiral axis. The labial side grows slightly faster than the lingual side, and its odontoblasts secrete Ca along the spiral axis and toward the pulp cavity at the same time. Thus the resultant direction of growth is more nearly opposite the extension of the occlusal end on the labial side, and Ca is consequently deposited over a wider area relative to that on the lingual surfaces. On the lingual side, Ca is deposited within a more limited area, and growth must therefore be continuous at high frequencies. The distribution of Ca on both sides of the tooth reflects these differences in growth rate and periodicity in two ways. First, given a unit area of tooth, the calcium concentration on the labial side is less than that of the lingual side. Second, whereas the calcium concentration on the labial side declines rapidly from the enamel-dentin junction to the pulp cavity, it is uniformly high across the lingual side because its growth is more continuous at high frequencies.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02408520
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  • 4
    Electronic Resource
    Electronic Resource
    Rhythmic dentinogenesis in the rabbit incisor: Circadian, ultradian, and infradian periods (1980)
    Springer
    Calcified tissue international 32 (1980), S. 29-44 
    Details
    ISSN: 1432-0827
    Keywords: Rabbit ; Dentin ; Calcium ; Sulfur ; Periodicity ; Circadian ; Ultradian
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary We have identified a variety of biological rhythms involved in the apposition and mineralization of dentin in the rabbit incisor. Animals were injected during the day or night with lead acetate at 2-week intervals—to provide biological time markers in forming dentin—and transverse undecalcified sections of the lower incisors were prepared for electron microprobe analysis. The positions of the lead markers were identified, and the continuous distribution of calcium and sulfur was measured at 1 µm intervals between the markers. In thin sections stained with hematoxylin after decalcification, the widths of a series of structural increments (bands) were measured with an ocular micrometer. Fourier analysis of the data revealed spectra of structural and compositional rhythms with a range of periodicities which extended from a matter of hours [ultradian (〈24 h)] to days [infradian (〉24 h) and circadian (approximately 24 h)]. The structural and compositional rhythms appeared to be independent to the extent that they did not necessarily have the same periods, or amplitudes. Nor were there simple phase relationships between all of the rhythms. At some times, Ca and S fluctuations are inversely proportional (180° out of phase), but in other cases they are directly proportional or out of phase by varying degrees other than 180°. The analyses thus suggest that calcium and sulfur deposition (representing mineral and glycosaminoglycan deposition, respectively) are not simply inversely proportional, and that the hematoxylin-stained structural increments did not solely reflect differences in the distribution of the mineral components in dentin.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02408519
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  • 5
    Electronic Resource
    Electronic Resource
    The inhibitory effect of cartilage proteoglycans on hydroxyapatite growth (1984)
    Springer
    Calcified tissue international 36 (1984), S. 285-290 
    Details
    ISSN: 1432-0827
    Keywords: Proteoglycans ; Chondroitin 4-sulfate ; Neutral dextran ; Hydroxyapatite growth
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary The calcification of connective tissues, including cartilage, is under the control of many interacting systems. Proteoglycans are thought to retard the deposition of hydroxyapatite crystals, and modification of the proteoglycans presumably facilitates mineralization in those tissues that are actively calcifying. The mechanism underlying these regulations remains speculative. This study investigates this question by comparing the inhibitory effectiveness of several macromolecules at neutral pH and approximately physiological ionic strengths. Inhibitors tested include bovine nasal proteoglycan monomer A1D1D1 and aggregate-containing A1 fractions, glycosaminoglycan chains (chondroitin 4-sulfate), and neutral dextran (as an uncharged analog). Hydroxyapatite growth was assessed either by measuring the time-dependent decreases in solution calcium and phosphate concentrations, or by determining utilization of hydroxyl ion in a pH-Stat. All species studied inhibit hydroxyapatite growth, and the extent of inhibition for each class is concentration-dependent. The proteoglycan aggregate-containing A1 fraction is more effective than the proteoglycan monomer at the same concentration, and the proteoglycan monomer is more effective than chondroitin 4-sulfate. Neutral dextran inhibits hydroxyapatite growth less effectively than proteoglycans. These results suggest that inhibition of hydroxyapatite growth by proteoglycans critically depends on both status (aggregate, monomer, etc.) and hydrodynamic size of this macromolecule, supporting the hypothesis that modification of proteoglycansin vivo functions to modulate the effectiveness of proteoglycans as a hydroxyapatite growth inhibitor.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF02405332
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  • 6
    Electronic Resource
    Electronic Resource
    Effect of proteoglycans on in vitro hydroxyapatite formation (1979)
    Springer
    Calcified tissue international 27 (1979), S. 75-82 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF02441164
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  • 7
    Electronic Resource
    Electronic Resource
    Age-Related changes in cartilage proteoglycans: Quantitative electron microscopic studies (1994)
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 28 (1994), S. 398-408 
    Details
    ISSN: 1059-910X
    Keywords: Aging ; Proteoglycans ; Electron microscopy ; Intervertebral disc ; Hyaline cartilage ; Nucleus pulposus ; Life and Medical Sciences ; Cell & Developmental Biology
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Natural Sciences in General
    Notes: Biochemical and biophysical studies have shown that the composition and sedimentation velocity of cartilage proteoglycans change with age, but these investigations cannot demonstrate the alterations in molecular structure responsible for these changes. Development of quantitative electron microscopic methods has made it possible to define the age-related structural changes in aggregating proteoglycans and to correlate the alterations in their structure with changes in tissue composition and morphology. Electron microscopic measurement of human and animal hyaline cartilage proteoglycans has shown that with increasing age the length of the chondroitin sulfate-rich region of aggregating proteoglycan monomers (aggrecan molecules) decreases, the variability in aggrecan length increases, the density of aggrecan keratan sulfate chains increases, the number of monomers per aggregate decreases, and the proportion of monomers that aggregate declines. Proteoglycans from the nucleus pulposus of the intervertebral disc show similar but more dramatic age-related alterations. At birth, nucleus pulposus aggrecan molecules are smaller and more variable in length than those found in articular cartilage. Within the first year of human life, the populations of aggregates and large aggrecan molecules analogous to those found in articular cartilage decline until few if any of these molecules remain in the central disc tissues of skeletally mature individuals. The mechanisms of the age-related changes in cartilage proteoglycans have not been fully explained, but measurement of proteoglycans synthesized by chondrocytes of different ages suggests that alterations in synthesis produce at least some of the age-related changes in aggrecan molecules. Degradation of aggrecan chondroitin sulfate-rich regions in the matrix probably also contributes to the structural changes seen by electron microscopy. Age-related changes in proteoglycan aggregation may be due to alterations in link protein function or inhibition of aggregation of newly synthesized aggrecan molecules by accumulation of degraded aggrecan molecules. © 1994 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/jemt.1070280506
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  • 8
    Electronic Resource
    Electronic Resource
    Neuerungen auf dem Thioindigorot-gebiet (1908)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 21 (1908), S. 961-970 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19080212002
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  • 9
    Electronic Resource
    Electronic Resource
    Carbene in räumlich begrenzten Systemen I. 1,3-C-H-Insertionsreaktion von Adamantyliden im β-Cyclodextrin-HohlraumCarbene Rearrangements, 41. Mitteilung. Wir danken der American Maize-Products Company, Hammond, IN, für die in dieser Untersuchung verwendeten Cyclodextrine. - 40. Mitteilung: L.Xu, G. Lin, F. Tao, U. H. Brinker, Acta Chem. Scand. 1992, 46, 650.Professor Emanuel Vogel zum 65. Geburtstag gewidmet. (1993)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 105 (1993), S. 1427-1429 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 1 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19931050943
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  • 10
    Electronic Resource
    Electronic Resource
    Über Küpenfarbstoffe (1909)
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 22 (1909), S. 2129-2131 
    Details
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/ange.19090224402
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