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  • Articles: DFG German National Licenses  (3)
  • 1990-1994  (3)
  • 1955-1959
  • tetradecyltrimethylammoniumsalicylate  (2)
  • Carp  (1)
Source
  • Articles: DFG German National Licenses  (3)
Material
Years
  • 1990-1994  (3)
  • 1955-1959
Year
  • 1
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 268 (1990), S. 460-468 
    ISSN: 1435-1536
    Keywords: Spinnability ; viscoelasticsurfactantsolution ; tetradecyltrimethylammoniumsalicylate ; hexadecyltrimethylammonium salicylate ; rodlikemicelle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Colloid & polymer science 270 (1992), S. 249-258 
    ISSN: 1435-1536
    Keywords: Viscoelasticity ; spinnability ; tetradecyltrimethylammoniumsalicylate ; hexadecyltrimethylammoniumsalicylate ; rodlikemicelle
    Source: Springer Online Journal Archives 1860-2000
    Topics: Chemistry and Pharmacology , Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
    Notes: 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.
    Type of Medium: Electronic Resource
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  • 3
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Myosin ; Myosin heavy chain ; ATPase activity ; Carp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: 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.
    Type of Medium: Electronic Resource
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