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  • Life Sciences (general)  (5)
  • Proteoglycans  (5)
  • General Chemistry  (4)
  • 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
    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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  • 4
    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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  • 5
    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
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  • 6
    Electronic Resource
    Electronic Resource
    Weinheim : Wiley-Blackwell
    Zeitschrift für die chemische Industrie 21 (1908), S. 961-970 
    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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  • 7
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 12 (1992), S. 311-317 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The excretion, cellular distribution and pH profiles of invertase in Aspergillus niger CCM 8004 were characterized. An optimized pH control was proposed for conversion of sucrose to gluconic acid and fructose: pH was maintained at 4.5 until the 12th hour and at 5.5 from the 12th hour of fermentation. 300 g · dm3 of sucrose was converted within 31 hours by this procedure.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 8
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 13 (1993), S. 269-274 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The basic parameters were studied influencing the conversion of orbitol to sorbose by Gluconobacter oxydans(industrial strain from FARMAKON Co., Czechoslovakia). The most effective conversion in the stationary phase was reached at pH 5.0, no inhibitory effect of sorbitol in a concentration ranging from 20 to 200 g/l and a minimum inhibitory effect of the sorbose concentration up to 200 g/l were observed. According to the optimum conditions mentioned above the optimized course of the fed-batch cultivation was proposed. The final concentration of sorbose of 410 g/l was reached after 36 hours.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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  • 9
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: Permeabilized cells of Kluyveromyces marxianus CCY eSY2 were tested as the source of lactase in the ethanol fermentation of concentrated deproteinized whey (65-70 g/l lactose) by Saccharomyces cerevisiae CCY 10-13-14. Rapid lactose hydrolysis by small amounts of permeabilized cells following the fermentation of released glucose and galactose by S. cerevisiae resulted in a twofold enhancement of the overall volumetric productivity (1.03 g/l × h), compared to the fermentation in which the lactose was directly fermented by K. marxianus.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
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  • 10
    Electronic Resource
    Electronic Resource
    Berlin : Wiley-Blackwell
    Acta Biotechnologica 15 (1995), S. 367-374 
    ISSN: 0138-4988
    Keywords: Life Sciences ; Life Sciences (general)
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Process Engineering, Biotechnology, Nutrition Technology
    Notes: The influence of basic physiological factors on the quality of inocula and L(+)-lactic acid production by Rhizopus arrhizus CCM 81 09 were studied.The most effective preparation of the spores (5 × 107 spores/ml) and subsequent good lactate production was achieved on the agar medium with soil extract and malt agar. The optimum initial amount of active spores for inoculation was 103-104 spores/ml. The preparation of inoculum required intensive stirring with lower aeration and pH maintained in the range from 4.8 to 6.0 by the addition of CaCO3. The maximum yield of lactic acid production was achieved by using 5% (v/v) of 24-h-old inoculum. The intensity of lactic acid production in the inoculum was proportional to its production in the subsequent steps of fermentation and can be used as a fast control of the physiological state of the producers.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
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