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  • 1990-1994  (2)
  • 1
    Electronic Resource
    Electronic Resource
    Stability of the Thrombolytic Protein Fibrolase: Effect of Temperature and pH on Activity and Conformation (1991)
    Springer
    Pharmaceutical research 8 (1991), S. 1103-1112 
    Details
    ISSN: 1573-904X
    Keywords: circular dichroism ; metalloprotein ; protein activity ; protein stability ; protein structure ; thrombolytic
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract The effect of temperature and pH on the activity and conformation of the thrombolytic protein fibrolase was examined. Fibrolase maintained proteolytic activity over 10 days at room temperature (∼22°C). At 37°C, greater than 50% of the proteolytic activity was lost within 2 days and no activity remained after 10 days. Circular dichroism (CD) spectra at elevated temperatures showed that alphahelical structure was lost in a cooperative transition (T m of 50°C at pH 8). Structural changes were detected by NMR prior to unfolding which were not observable by CD, and the T m determined by NMR was 46°C at pD 8. The effect of pH on the proteolytic activity and structure of fibrolase was examined over the pH range from 1 to 10. Activity was maintained at neutral to alkaline pH values from pH 6.5 to pH 10.0 but decreased substantially in acidic media. While CD spectra indicated little variation in secondary structure over the pH range 5 to 9, significant differences were noted at pH 2 to 3. The melting temperature of fibrolase decreased to 43°C at pH 5. Protein concentrations determined over the pH range 1 to 10 showed an apparent solubility minimum at pH 5.0, which did not correspond to the isoelectric point of 6.5. Explanations for these observations are proposed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015842032164
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  • 2
    Electronic Resource
    Electronic Resource
    Effect of Zinc Binding on the Structure and Stability of Fibrolase, a Fibrinolytic Protein from Snake Venom (1992)
    Springer
    Pharmaceutical research 9 (1992), S. 870-877 
    Details
    ISSN: 1573-904X
    Keywords: fibrolase ; metalloprotease ; zinc binding ; enzyme ; sequence ; protein structure
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology
    Notes: Abstract Fibrolase is a metalloprotease with potential use as a fibrinolytic agent. Loss of the intrinsic zinc atom leads to a rapid decrease in enzymatic activity. Circular dichroism measurements indicate that there is a partial unfolding of an α-helical section of the protein concomitant with the loss of zinc. Removal of zinc can be affected by elevated temperatures, acidic pH values, and addition of chelating agents. At low molar concentrations, both ethylenediaminetet-raacetic acid (EDTA) and dithiothreitol (DTT) were found to remove zinc efficiently. Analysis of the sequence of fibrolase identified a segment which possessed a high degree of homology with the metal binding site of other zinc proteases, such as thermolysin and the collagenases. However, the putative zinc binding site in fibrolase lacks the additional glutamate ligand found in thermolysin and subtilisin. This sequence is also predicted to adopt an α-helical conformation. Together, these data indicate that there is a well-defined metal binding site in fibrolase and that metal binding is the most important factor governing the stability of this protein.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1015840613799
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    Paper (German National Licenses)
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