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  • 1990-1994  (3)
  • 1965-1969
  • 1960-1964
  • 1955-1959
  • rodlikemicelle  (2)
  • Carp  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Colloid & polymer science 270 (1992), S. 249-258 
    ISSN: 1435-1536
    Schlagwort(e): Viscoelasticity ; spinnability ; tetradecyltrimethylammoniumsalicylate ; hexadecyltrimethylammoniumsalicylate ; rodlikemicelle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie , Maschinenbau
    Notizen: Abstract The viscoelasticity has been measured for aqueous solutions of tetradecyl-and hexadecyltrimethylammonium salicylates (C14TASal, C16TASal). The aqueous solutions of C14TASal without salt displayed the gel-like behavior at 10.0×10−2 g cm−3, but those more dilute than 3.2×10−2 g cm−3 presented the viscoelasticity similar to that of a Maxwell liquid. The Maxwell-like behavior was converted to the polymer-like one on the addition of (0.1–0.2) M NaBr or (0.02–0.2) M NaSal. The gel-like viscoelasticity can be connected with the spinnability of “cohesive fracture failure”, and the Maxwell-like and polymer-like viscoelasticities are concerned with the spinnability of “ductile failure”. The gel-like and Maxwell-like viscoelasticities originate in the pseudo-network formed by the pseudo-linkages between rodlike micelles, while the polymer-like viscoelasticity is caused by the entanglement of long rodlike micelles in semidilute and concentrated solutions. The aqueous solutions of C16TASal behaved very similar to those of C14TASal.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Colloid & polymer science 268 (1990), S. 460-468 
    ISSN: 1435-1536
    Schlagwort(e): Spinnability ; viscoelasticsurfactantsolution ; tetradecyltrimethylammoniumsalicylate ; hexadecyltrimethylammonium salicylate ; rodlikemicelle
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Chemie und Pharmazie , Maschinenbau
    Notizen: Abstract The spinnability was measured for aqueous viscoelastic solutions of tetradecyl- and hexadecyltrimethylammonium salicylates (C14TASal, C16TASal) in the absence and presence of sodium salicylate (NaSal) and sodium bromide (NaBr). The spinnability is classified into two types, D and C. While the intrinsic drawing length in type D is proportional to the drawing velocity, the drawing intrinsic length in type C decreases with the drawing velocity or is independent of it. The spinnability changes from type D to C, as the drawing velocity and the surfactant concentration increase, and the temperature lowers. The effect of salt is different between NaSal and NaBr. It can be assumed that a pseudo-network structure composed of rod-like micelles is formed in viscoelastic and spinnable surfactant solutions. Then, the spinnability depends on the balance between the elasticity and the viscosity in which the structure results.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    ISSN: 1432-136X
    Schlagwort(e): Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Medizin
    Notizen: Summary Myosins were isolated from dorsal ordinary muscles of carp acclimated to 10°C and 30°C for a minimum of 5 weeks and examined for their ATPase activities. Ca2+-ATPase activity was different between myosins from cold-and warm-acclimated carp, especially at KCl concentrations ranging from 0.1 to 0.2 M, when measured at pH 7.0. The highest activity was 0.32 μmol Pi·min-1·mg-1 at 0.2 M KCl for cold-acclimated carp and 0.47 μmol Pi·min-1·mg-1 at 0.1 M KCl for warm-acclimated fish. The pH-dependency of Ca2+-ATPase activity at 0.5 M KCl for both carp was, however, similar exhibiting two maxima around 0.3 μmol Pi·min-1·mg-1 at pH 6 and 0.4 μmol Pi·min-1·mg-1 at pH 9. K+(EDTA)-ATPase activity at pH 7.0 neither exhibited differences between both myosins. It increased with increasing KCl concentration showing the highest value of about 0.4 μmol Pi·min-1·mg-1 at 0.6–0.7 M KCl. Actin-activated myosin Mg2+-ATPase activity was markedly different between cold-and warm-acclimated carp. The maximum initial velocity was 0.53 μmol Pi·min-1·mg-1 myosin at pH 7.0 and 0.05 M KCl for cold-acclimated carp, which was 1.6 times as high as that for warm-acclimated carp. These differences were in good agreement with those obtained with myofibrillar Mg2+-ATPase activity between both carp. No differences were, however, observed in myosin affinity to actin. Differences in myosin properties between cold- and warm-acclimated carp were further evidenced by its thermal stability. The inactivation rate constant of myosin Ca2+-ATPase was 25·10-4·s-1 at 30°C and pH 7.0 for cold-acclimated carp, which was about 4 times as high as that for warm-acclimated carp. Light chain composition did not differ between both carp myosins. The differences in a primary structure of the heavy chain subunit was, however, clearly demonstrated between both myosins by peptide mapping.
    Materialart: Digitale Medien
    Bibliothek Standort Signatur Band/Heft/Jahr Verfügbarkeit
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