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  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 51 (1992), S. 213-217 
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Degradation of amelogenin ; Proteinases ; 25kDa amelogenin ; Enzymography
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Summary In the outermost layer of porcine-developing enamel adjacent to the ameloblasts in the secretory stage, the activities of two proteinases having molecular masses of 76 and 78kDa were detected by enzymography using gelatin as a substrate. On the other hand, high activities of known 30 and 34kDa proteinases were localized in the inner layer of the enamel. The 76kDa proteinase cleaved the carboxylterminal peptide of porcine 25kDa amelogenin to convert it to 20kDa amelogenin. The 78kDa proteinase also acted on the 25kDa amelogenin similarly, but its activity was weak. The results indicate that the 25kDa amelogenin synthesized and secreted by ameloblasts is converted to 20kDa amelogenin by the action of proteinase localized in the outermost layer of the secretory enamel, and then further degraded by the proteinases in the inner layer of the enamel associated with the increase of mineralization.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Calcified tissue international 54 (1994), S. 69-75 
    ISSN: 1432-0827
    Keywords: Porcine secretory enamel ; Porcine amelogenin ; Plasma desorption mass spectometry ; Amino acid sequence ; CNBr cleavage
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine , Physics
    Notes: Abstract Amelogenins were extracted from the thin outer layer of porcine secretory enamel and purified by gel filtration and reverse-phase HPLC. The results of amino acid sequencing of the purified porcine amelogenins indicated the presence of at least four prototype amelogenins translated from alternatively spliced transcripts. The results of mass spectroscopy of the CNBr-cleaved peptides derived from the 25kDa amelogenin indicated that porcine 25kDa amelogenin is neither phosphorylated nor glycosylated.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    World journal of microbiology and biotechnology 16 (2000), S. 187-194 
    ISSN: 1573-0972
    Keywords: Active oxygen ; antibacterial activity ; ceramic ; magnesium oxide
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract The antibacterial activity of magnesium oxide (MgO) was studied. Inhibitory zones appeared around the MgO powder slurry put directly on nutrient agar plates seeded with Escherichia coli or Staphylococcus aureus. However, no zone was observed using a penicillin cup to avoid contact between the bacteria and the MgO powder. Moreover, the supernatant solution of the MgO powder slurry and a MgCl2 solution containing Mg2+ at a concentration of the solubility of MgO did not affect the growth of E. coli and S. aureus. Moreover, elevated shaking speed increased the death of E. coli in the slurry, indicating that the contact frequency between bacterial cells and MgO powders affected the antibacterial activity. It was considered that the contact between MgO powder and bacteria was important for the occurrence of its antibacterial activity. Since the generation of active oxygen, such as O2 −, from the MgO powder slurry was detected by chemiluminescence analysis, an investigation was carried out to determine whether active oxygen generated from MgO powder slurry was related to its antibacterial activity. The changes in the antibiotic sensitivity in E. coli treated by MgO powder agreed with those by active oxygen treatment. These results suggested that the active oxygen generated from the MgO powder slurry was one of the primary factors in its antibacterial activity.
    Type of Medium: Electronic Resource
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