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  • 1
    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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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 36 (1984), S. 285-290 
    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
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  • 3
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 5 (1922), S. 575-576 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 11 (1928), S. 731-750 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: L'étude de la conductibilité des silicates aux températures élevées peut servir à déceler et à suivre des réactions dont ces silicates peuvent être le siège.
    Additional Material: 4 Tab.
    Type of Medium: Electronic Resource
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  • 5
    Electronic Resource
    Electronic Resource
    New York, NY : Wiley-Blackwell
    Helvetica Chimica Acta 18 (1935), S. 721-724 
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 6
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 7
    ISSN: 0018-019X
    Keywords: Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Additional Material: 2 Tab.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Chirality 2 (1990), S. 275-279 
    ISSN: 0899-0042
    Keywords: nucleotide analogue ; antiviral ; chiral separation ; complexation ; ion-pairing ; Chemistry ; Organic Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: An acylonucleotide analogue, 1-[3-hydroxy-2-(phosphonyl-methoxy)propyl]cytosine (HPMPC), has shown activity against herpes simplex Type I and Type II viruses. An HPLC separation of the R- and S-enantiomers of HPMPC by ligand exchange using a mobile phase containing phenylalanine as the chiral modifier and copper(II) as the metal ion is reported.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
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  • 9
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 22 (1909), S. 2129-2131 
    ISSN: 0044-8249
    Keywords: Chemistry ; General Chemistry
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    New York, NY [u.a.] : Wiley-Blackwell
    Microscopy Research and Technique 28 (1994), S. 398-408 
    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
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