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  • Digitale Medien  (4)
  • 1990-1994  (4)
  • 1960-1964
  • rodlikemicelle  (2)
  • Bloodstains  (1)
  • Carp  (1)
  • 1
    Digitale Medien
    Digitale Medien
    Polymorphism of coagulation factor XIII B subunit: Further occurrence of FXIIIB*15 in Japanese and phenotyping in bloodstains (1992)
    Springer
    International journal of legal medicine 104 (1992), S. 317-319 
    Details
    ISSN: 1437-1596
    Schlagwort(e): Polymorphism FXIIIB ; Population genetics ; Bloodstains ; Polymorphismus FXIIIB ; Populationsgenetik ; Blutspuren
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Medizin , Rechtswissenschaft
    Beschreibung / Inhaltsverzeichnis: Zusammenfassung Der Polymorphismus des FXIIIB wurde bei 555 unverwandten Japanern mit Hilfe der isoelektrischen Fokussierung und anschließendem Immunoblotting untersucht. Fünf allgemein vorkommende Phänotypen und die seltene Variante FXIIIB 15-3 wurden beobachtet. Die Allel-Frequenzen waren FXIIIB = 0,3063, FXIIIB2 = 0,0162, FXIIIB3 = 0,6766 und FXIIIB15 = 0,0009. Die Bestimmung der Phänotypen war auch an Blutspuren mit folgenden Lagerungsbedingungen möglich: Bei 37°C über einen Zeitraum bis zu 4 Monate, bei Raumtemperatur und bei 4°C länger als 6 Monate. Das FXIIIB-System kann einen neuen, aussagekräftigen genetischen Marker für gerichtsmedizinische Blutspurenuntersuchungen darstellen.
    Notizen: Summary The polymorphism of FXIIIB was investigated in 555 unrelated Japanese individuals using isoelectric focusing and immunoblotting. Five common phenotypes and a rare variant type FXIIIB 15-3 were observed. The allele frequencies were FXIIIB*1 = 0.3063, FXIIIB*2 = 0.0162, FXIIIB*3 = 0.6766 and FXIIIB*15 = 0.0009. Phenotyping was also possible from bloodstains stored at 37°C for up to 4 months and from bloodstains stored at room temperature and at 4°C for over 6 months. The FXIIIB system can provide a new powerful genetic marker for the medicolegal grouping of bloodstains.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1007/BF01369549
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  • 2
    Digitale Medien
    Digitale Medien
    The viscoelasticity of spinnable solutions of alkyltrimethylammonium salicylates (1992)
    Springer
    Colloid & polymer science 270 (1992), S. 249-258 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00655477
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  • 3
    Digitale Medien
    Digitale Medien
    The spinnability of viscoelastic solutions of tetradecyl- and hexadecyl-trimethylammonium salicylates (1990)
    Springer
    Colloid & polymer science 268 (1990), S. 460-468 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF01411005
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  • 4
    Digitale Medien
    Digitale Medien
    Changes in carp myosin ATPase induced by temperature acclimation (1990)
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00302588
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