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  • 1990-1994  (2)
  • Solubility  (1)
  • protease  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Effect of pressure on the solubility of naphthalene in water at 25°C (1993)
    Springer
    Journal of solution chemistry 22 (1993), S. 727-732 
    Details
    ISSN: 1572-8927
    Schlagwort(e): Solubility ; high pressure ; hydrophobic hydration ; partial molar volume ; naphthalene
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie
    Notizen: Abstract Solubility of naphthalene in water was measured at 25°C and pressures up to 200 MPa. The solubility decreased with increasing pressure. From the pressure coefficient of the solubility, the volume change ΔV accompanying the dissolution was estimated as 13.8±0.4 cm 3 -mol −1 . Further we estimated the volume change ΔV CH accompanying hydrophobic hydration as −0.1±0.6 cm 3 -mol −1 using the ΔV value, the molar volume of crystalline naphthalene, and the partial molar volume of naphthalene in n-heptane. This ΔV CH is much larger (i.e., less negative) than that for hydrophobic hydration of alkyl-chain compounds and suggests that the hydration structure of naphthalene differs from that of alkyl-chain compounds.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF00647412
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  • 2
    Digitale Medien
    Digitale Medien
    Chymotrypsin-like and trypsin-like protease activities in the sea urchin (Hemicentrotus pulcherrimus) egg (1992)
    Springer
    Cellular and molecular life sciences 48 (1992), S. 287-290 
    Details
    ISSN: 1420-9071
    Schlagwort(e): Sea urchin egg ; protease ; trypsin ; chymotrypsin ; fertilization
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Abstract Proteolytic activities in extracts of sea urchin eggs were examined using SDS (sodium dodecyl sulphate)-polyacrylamide gels. In the unfertilized eggs, proteases were detected as bands corresponding to the molecular weights of 40 kD and 26 kD on the gelatin gel, and 35 kD and 30 kD on the casein gel. Using various protease inhibitors, it was found that 40 kD, 30 kD, and 26 kD are chymotrypsin-like proteases and that 35 kD is a trypsin-like protease. The activity of the 40 kD chymotrypsin-like protease was found to be almost completely lost after insemination.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01930478
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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    Artikel (Nationallizenzen)
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