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  • Electronic Resource  (2)
  • 1990-1994  (2)
  • 1955-1959
  • Bloodstains  (1)
  • Carp  (1)
  • 1
    Electronic Resource
    Electronic Resource
    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
    Keywords: Polymorphism FXIIIB ; Population genetics ; Bloodstains ; Polymorphismus FXIIIB ; Populationsgenetik ; Blutspuren
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine , Law
    Description / Table of Contents: 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.
    Notes: 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.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01369549
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    Paper (German National Licenses)
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  • 2
    Electronic Resource
    Electronic Resource
    Changes in carp myosin ATPase induced by temperature acclimation (1990)
    Springer
    Journal of comparative physiology 160 (1990), S. 233-239 
    Details
    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
    URL: http://dx.doi.org/10.1007/BF00302588
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    Paper (German National Licenses)
    Fulltext
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