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  • Carp  (1)
  • Cellular slime mold  (1)
  • Springer  (2)
  • Molecular Diversity Preservation International (MDPI)
  • MDPI Publishing
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  • Springer  (2)
  • Molecular Diversity Preservation International (MDPI)
  • MDPI Publishing
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  • 1
    ISSN: 1618-0860
    Keywords: Cell-cell adhesion ; Cellular slime mold ; Glycoprotein ; Polysphondylium pallidum ; Tunicamycin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract To assess the role in cell-cell adhesion of gp64, a putative cell-cell adhesion molecule ofPolysphondylium pallidum, we treated the cells with tunicamycin (TM), a known inhibitor of the synthesis of the N-linked oligosaccharide precursor, and examined TM's effect on cell-cell adhesion. The vegetative growth ofPolysphondylium cells was inhibited with TM in a dose-dependent manner. When cells were treated with TM (2.0 μg/ml) during only the first 4 hr of starvation and further starved for 8 hr without TM, the cells dissociated considerably, although even the growth phase cells ofPolysphondylium normally show EDTA-resistant (Ca2+-independent) cell adhesions. In parallel with the above effects, the amounts of intact gp64 decreased considerably in time with the lengths of incubation (0 hr〉4 hr 〉8 hr). When TM-treated cells were washed free of TM, and shaken for a further 12 hr, the cells began to aggregate again, accompanied by an increase of gp64. In conclusion, TM affected cell-cell adhesion ofPolysphondylium cells, but we were not able to distinguish whether the inhibition of cell aggregation was due to defects in glycosylation on glycoproteins and/or due to reduced levels of glycoproteins themselves.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    Springer
    Journal of comparative physiology 161 (1991), S. 141-146 
    ISSN: 1432-136X
    Keywords: Temperature ; Acclimation ; Carp ; Myosin ; Myosin subfragment-1 ; ATPase activity ; Thermostability
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology , Medicine
    Notes: Summary Heavy meromyosin subfragment-1 (S1) was prepared by α-chymotrypsin from myosin of carp acclimated to either 10°C or 30°C for a minimum of 5 weeks. The objective of these studies was to document thermally-induced changes in the myosin molecule and to extend previous observations. Ca2+- and K+ (EDTA)-ATPase activities of cold-acclimated carp S1 were 1.1 and 0.8 μmol Pi·min-1·mg-1, respectively, and these values did not differ significantly from those of warm-acclimated carp. The inactivation rate constant (KD) of S1 from cold-acclimated carp was 32.1x10-4· s-1, compared to 13.2x10-4·s-1 for warm-acclimated carp. The maximum initial velocity of acto-S1 Mg2+-ATPase activity at pH 7.0 in 0.05 M KCl was 9.3 s-1 with cold-acclimated carp, about 3.7 times higher than that for warm-acclimated carp. However, no significant difference was observed in the apparent affinity of S1 to actin. Peptides maps of the heavy chain of S1 were different and suggested distinct isoforms for the myosins from warm- and cold-acclimated muscle.
    Type of Medium: Electronic Resource
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