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  • 1
    Electronic Resource
    Electronic Resource
    Prediction of solid-state amorphizing reaction using effective driving force (1995)
    [S.l.] : American Institute of Physics (AIP)
    Journal of Applied Physics 78 (1995), S. 983-987 
    Details
    ISSN: 1089-7550
    Source: AIP Digital Archive
    Topics: Physics
    Notes: It is proposed that the nucleation and growth of the amorphous phase through the solid-state amorphizing reaction in thin-film diffusion couples can be predicted by using the concept of effective driving force. The effective driving force consists of two factors: (i) the thermodynamic driving force given by maximum free-energy difference between the physical mixture of binary elements and the amorphous phase (ΔGmax), and (ii) the kinetic factor given by a ratio of the effective radius of the interstitial site in the host matrix to the atomic radius of the diffusing species (Rm/d). From the comparison of reported experimental results, it is shown that the criterion of effective driving force holds well for predicting the nucleation of the amorphous phase in metal/silicon systems as well as that of metal/metal systems. In addition, the concept of effective driving force holds well for predicting the growth tendency of the amorphous phase in metal/silicon systems. © 1995 American Institute of Physics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1063/1.360292
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  • 2
    Electronic Resource
    Electronic Resource
    Anti-elastase and anti-hyaluronidase of phenolic substance from Areca catechu as a new anti-ageing agent (2001)
    Oxford, UK : Blackwell Science, Ltd
    International journal of cosmetic science 23 (2001), S. 0 
    Details
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: Synopsis We have previously screened 150 medicinal plants for the inhibition of elastase and found significant inhibitory effects of the extracts of Areca catechu L. on the ageing and inflammation of skin tissues. To isolate and identify the compounds having biological activity, they were further purified by each fraction of solvents, silica gel column chromatography, preparative TLC and reversed-phase HPLC. The peak in HPLC, which coincided with the inhibitory activity against elastase, was identified as a phenolic substance by using various colorimetric methods, UV and IR. IC50 values of this phenolic substance were 26.9 μg mL−1 for porcine pancreatic elastase (PPE) and 60.8 μg mL−1 for human neutrophil elastase (HNE). This phenolic substance showed more potent activity than that of reference compounds, oleanolic acid (76.5 μg mL−1 for PPE, 219.2 μg mL−1 for HNE) and ursolic acid (31.0 μg mL−1 for PPE, 118.6 μg mL−1 for HNE). According to the Lineweaver–Burk plots, the inhibition against both PPE and HNE by this phenolic substance was competitive inhibition with the substrate. The phenolic substance from A. catechu effectively inhibited hyaluronidase activity (IC50 : 210 μg mL−1 ).These results suggest that the phenolic substance purified from A. catechu has an anti-ageing effect by protecting connective tissue proteins.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.0412-5463.2001.00102.x
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  • 3
    Electronic Resource
    Electronic Resource
    Inhibitory Effects of 150 Plant Extracts on Elastase Activity, and Their Anti-inflammatory Effects (1999)
    Dordrecht, The Netherlands : Blackwell Science Ltd
    International journal of cosmetic science 21 (1999), S. 0 
    Details
    ISSN: 1468-2494
    Source: Blackwell Publishing Journal Backfiles 1879-2005
    Topics: Medicine
    Notes: The inhibitory effects of 150 medicinal plants on elastase activity were investigated. Among the 150 plants, six plant extracts (final concentration 1 mg/ml in methanol) exhibited more than 65% of inhibition of elastase activity. The inhibitory effects of six active plants, including Areca catechu (IC50, 42.4 μg/ml), Cinnamonum cassia (IC50, 208.7 μg/ml), Myristica fragrans (IC50, 284.1 μg/ml), Curcuma longa (IC50, 398.4 μg/ml), Alpinia katsumadai (IC50, 465.7 μg/ml) and Dryopteris cassirrhizoma (IC50, 714.4 μg/ml) on the activity of human leukocyte elastase, hyaluronidase and lipid peroxidation were examined. In the lipid peroxidation assay, using the TBA method, three of the six plants, including Curcuma longa (IC50, 45.5 μg/ml), Areca catechu (IC50, 51.0 μg/ml) and Alpinia katsumadai (IC50, 116.3 μg/ml) exhibited more than 70% inhibition at the concentration of 1 μg/ml, but only one plant, Areca catechu (IC50, 563 μg/ml) showed high inhibitory effect on hyaluronidase activity. The results suggest that medicinal plants showing several biological activities may be potent inhibitors of the anti-ageing process in skin. This property might be useful for application in cosmetics.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1046/j.1467-2494.1999.181638.x
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  • 4
    Electronic Resource
    Electronic Resource
    The interaction of flavins with egg white riboflavin-binding protein
    Amsterdam : Elsevier
    Archives of Biochemistry and Biophysics 204 (1980), S. 41-51 
    Details
    ISSN: 0003-9861
    Source: Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
    Topics: Biology , Chemistry and Pharmacology , Physics
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1016/0003-9861(80)90005-3
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  • 5
    Electronic Resource
    Electronic Resource
    Purification and properties of intracellular fructosyl transferase fromAureobasidium pullulans (1992)
    Springer
    World journal of microbiology and biotechnology 8 (1992), S. 411-415 
    Details
    ISSN: 1573-0972
    Keywords: Aureobasidium pullulans ; fructo-oligosaccharide ; fructosyl transferase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Process Engineering, Biotechnology, Nutrition Technology
    Notes: Abstract Intracellular frustosyl transferase was purified fromAureobasidium pullulans C-23 by ethanol fractionation, CM-Sephadex chromatography and preparative disc gel electrophoresis. It was shown to be homogeneous on disc polyacrylamide gel electrophoresis, with a molecular size of 190kDa. The pI value of the enzyme was about 3.7. The enzyme has aK m value of 0.43 mM for sucrose and was optimally active at pH 5.0 and 60°C. The enzyme was stable from pH 2.5 to 12. It was almost completely inhibited by 5mM Hg2+ but was not significantly affected by other cations. The transferase was inactivated by treatment with the tryptophan-specific reagentN-bromosuccinimide and the tyrosine-specific reagent, I2, suggesting that tryptophan and tyrosine residues are probably located at or near the active site of the enzyme.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01198756
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