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  • Algae  (1)
  • Chemistry  (1)
  • Synchrony  (1)
  • 1
    ISSN: 1432-072X
    Keywords: Euglena ; Mutants ; Circadian rhythm ; Algae ; Biological clock ; Cell division ; Photosynthesis ; Cell cycle ; Thiols ; Synchrony
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Previous work has demonstrated a persisting, free-running, circadian rhythm of cell division in the P4ZUL photosynthetic mutant of the alga Euglena gracilis Klebs (Strain Z) Pringsheim grown organotrophically in continuous light or darkness at 19° C following prior synchronization by a repetitive LD: 10,14 light cycle. A similar circadian rhythmicity has been recently discovered in the W6ZHL heat-bleached and the Y9ZNalL naladixic acid-induced mutants of Euglena grown under comparable conditions. Over extended timespans, however, these mutants appear to gradually lose first their ability to display persisting overt rhythms, and then even their capability of being entrained by imposed LD cycles. These properties can be restored by the addition of certain sulfur-containing compounds to the medium including cysteine, methionine, dithiothreital, sodium monosulfide, sodium sulfite, and sodium thiosulfate, as well as thioglycolic [mercaptoacetic] acid. The implications of these findings toward biological clock mechanisms are discussed: It appears that some sort of coupling process is operating as opposed to the initiation of an underlying oscillation.
    Type of Medium: Electronic Resource
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  • 2
    Electronic Resource
    Electronic Resource
    New York : Wiley-Blackwell
    Biopolymers 21 (1982), S. 1411-1425 
    ISSN: 0006-3525
    Keywords: Chemistry ; Polymer and Materials Science
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Chemistry and Pharmacology
    Notes: Phosphorylase kinase contains four approximately equivalent binding sites for 1-anilinonaphthalene-8-sulfonate (1,8-ANS). Measurements of the time decay of fluorescence anisotropy have failed to give any indication of internal degrees of rotational freedom involving a significant portion of the tertiary structure. In the presence of 1 mM Ca2+, calmodulin binds one molecule of 1,8-ANS. No binding occurs in the absence of Ca2+. The binding is strongly temperature-dependent, a decrease in binding occurring with increasing temperature. Determinations of the time decay of fluorescence anisotropy indicate the presence of internal rotations, which become more important with increasing temperature. Complex formation between phosphorylase kinase and calmodulin reduces the binding of 1,8-ANS.
    Additional Material: 8 Ill.
    Type of Medium: Electronic Resource
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