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  • Electronic Resource  (4)
  • 1995-1999  (4)
  • 1970-1974
  • 1997  (4)
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  • Electronic Resource  (4)
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  • 1995-1999  (4)
  • 1970-1974
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  • 1
    Electronic Resource
    Electronic Resource
    College Park, Md. : American Institute of Physics (AIP)
    The Journal of Chemical Physics 107 (1997), S. 4436-4438 
    ISSN: 1089-7690
    Source: AIP Digital Archive
    Topics: Physics , Chemistry and Pharmacology
    Notes: We found that the Raman–Stokes shift of the C(Double Bond)N stretching mode of Phenol Blue changes with excitation energy; the frequency of this Raman band increased with an increase of the excitation energy, whereas the bandwidth was almost the same. The origin of the excitation energy dependence is discussed in connection with the correlation of the effect of the solvent fluctuation on the electronic transition energy and the vibrational frequency. © 1997 American Institute of Physics.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Mineralogy and petrology 61 (1997), S. 181-198 
    ISSN: 1438-1168
    Source: Springer Online Journal Archives 1860-2000
    Topics: Geosciences
    Description / Table of Contents: Zusammenfassung Die Fe- und Mn-Verteilung in Mineralen der Pumpellyit-Gruppe (W 8 X 4 Y 8 Z 12O56-n (OH)n) wurde mittels Mössbauer-Spektroskopie studiert. Die untersuchten Fe-Pumpellyite der Pumpellyit-Julgoldit-Serie stammen von zwei verschiedenen japanischen Lokalitäten: von Metabasiten des Tokoro-Gürtels, Hokkaido, und von Gabbro-Sills der Shimane Halbinsel. Okhotskit, ein Mn3+-dominiertes Mineral der Pumpellyit-Gruppe, wurde aus Erzen einer Mn-führenden Eisenerzlagerstätte des Tokoro-Gürtels separiert. Das57Fe Mössbauer-Spektrum der Tokoro Fe-Pumpellyite zeigt zwei Fe2+- und zwei Fe3+-Doubletten. Auf Grund bisher publizierter verfeinerter Einkristall-Strukturuntersuchungen von Al-Pumpellyiten werden diese Doubletten folgendermaßen zugeordnet: Fe W 2+ (IS = 1.01 undQS = 2.73 mm/s), Fe X 2+ (IS = 0.97 undQS = 3.18 mm/s), Fe X 3+ (IS = 0.29 undQS =1.37 mm/s) und Fe Y 3+ (IS = 0.36 undQS = 2.09 mm/s).IS bezeichnet dabei die Isomer-Shift relativ zu einem metallischen Eisenabsorbenten,QS das Quadrupole-Splitting. Diese Zuordnungen belegen den bevorzugten Einbau von Fe3+ in die X-Position. Das Mössbauer-Spektrum von Okhotskit zeigt zwei Doubletten bei Fe X 3+ (IS = 0.37 undQS = 1.13 mm/s) und Fe Y 3+ (IS = 0.42 undQS = 2.18 mm/s). Das Flächenverhältnis zeigt, daß das Verhältnis Fe X 3+ :Fe Y 3+ 94:6 ist. Auf Grund der chemischen und der Mössbauer-Analysen wird das Mn X 3+ :Mn Y 3+ Verhältnis mit 19:81 angegeben. Mn3+ zeigt somit eine stärkere Präferenz für die Y-Position als Fe3+, ein Resultat, das mit der Jahn-Teller-Theorie konsistent ist. Der bevorzugte Einbau in die Y-Position ist, in dieser Reihenfolge, Al〉Mn3+〉Fe3+.
    Notes: Summary Fe and Mn distribution in the pumpellyite group minerals (W 8 X 4 Y 8 Z 12056-n (OH) n ) has been studied by using57Fe Mössbauer spectroscopy. The studied Fe-pumpellyites, belonging to the pumpellyite-julgoldite series, were collected from two localities; metabasites in the Tokoro belt, Hokkaido, and gabbroic sills in the Shimane Peninsula, Japan. Okhotskite, an Mn3+-dominant pumpellyite group mineral, was separated from the ores of metamorphosed manganiferous iron ore deposits in the Tokoro belt.57Fe Mössbauer spectrum of Tokoro Fe-pumpellyite is composed of two Fe2+- and two Fe3+-doublets. On the basis of the single crystal structure refinements of Al-pumpellyites published so far, doublets were assigned to Fe W 2+ (IS= 1.01 andQS = 2.73 mm/s), Fe X 2+ (IS = 0.97 andQS = 3.18 mm/s), Fe X 3+ (IS = 0.29 andQS =1.37 mm/s) and Fe Y 3+ (IS = 0.36 andQS = 2.09 mm/s), whereIS is isomer shift relative to a metallic iron absorber andQS is quadrupole splitting. The Mössbauer spectrum of the Mitsu Fepumpellyite is composed of three doublets assigned to Fe X 2+ (IS= 1.14 andQS = 3.20 mm/s), Fe X 3+ (IS = 0.36 andQS =1.13 mm/s) and Fe Y 3+ (IS = 0.37 andQS= 1.93 mm/s). These assignments show strong preference of Fe3+ in the X-site. The Mössbauer spectrum of the okhotskite is composed of two doublets by Fe X 3+ (IS= 0.37 andQS = 1.13 mm/s) and Fe Y 3+ (IS = 0.42 andQS = 2.18 mm/s). The area ratio shows that Fe X 3+ :Fe Y 3+ ratio is 94:6. On the basis of chemical and Mössbauer analyses, Mn X 3+ :Mn Y 3+ ratio is given as 19:81, indicating stronger Y-site preference of Mn3+ than Fe3+, what is consistent with Jahn-Teller theory. Al, Mn3+ and Fe3+ prefer the Y-site in this order.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1573-675X
    Keywords: bcl-2 ; lpr ; T cell receptor (TCR)
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Abstract Autoimmune-prone lpr mice develop lymphoproliferative disorders, whereas their lymphocytes show accelerated apoptosis in culture. To elucidate whether the bcl-2 protein, a repressor of apoptosis, is critical to the discrepancy between in vivo and in vitro survival, we examined bcl-2 expression in T cells from +/+ and lpr mice during culture. The expression levels of bcl-2 in cultured T cells from lpr mice were significantly down-modulated compared to those from +/+ mice and freshly obtained T cells. Besides, the reduction of bcl-2 protein levels was inhibited in T cells cultured in the presence of T cell receptor (TCR) signalling. These results suggest that lpr T cells might be susceptible to apoptosis in vitro due to down-modulation of bcl-2 by withdrawal of TCR signalling.
    Type of Medium: Electronic Resource
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  • 4
    Electronic Resource
    Electronic Resource
    Springer
    Basic research in cardiology 92 (1997), S. 11-15 
    ISSN: 1435-1803
    Keywords: Phospholamban ; calcium ATPases, sarcoplasmic reticulum, phosphorylation
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract In an effort to define the amino acids that are involved in functional interactions between phospholamban (PLN) and the Ca2+ ATPase of cardiac sarcoplasmic reticulum (SERCA2), we have coexpressed wild type and mutant forms of phospholamban with wild type and mutant forms of SERCA2, isolated microsomal fractions and measured Ca2+ dependence of Ca2+ transport. We have found that both charged and hydrophobic residues in the cytoplasmic domains of both PLN and SERCA2 make up the cytoplasmic interaction site. In SERCA2, this site is the linear sequence Lys-Asp-Asp-Lys-Pro-Val402: In PLN, the site is more diffuse and complex. Function was retained if the net charge over the first 20 amino acids was +1 or +2, but function was lost if the net charge was −3, −2, 0 or +3. Function was also lost if the long alkyl side chains of Val4, Leu7 or Ile12 were replaced with the methyl group of Ala. We have also obtained evidence that a site of functional interaction is present in the transmembrane domains of PLN and SERCA2.
    Type of Medium: Electronic Resource
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