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  • reticulocyte maturation  (2)
  • Springer  (2)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
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Verlag/Herausgeber
  • Springer  (2)
  • American Institute of Physics
  • Copernicus
  • Public Library of Science
Erscheinungszeitraum
  • 1
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 85 (1989), S. 3-7 
    ISSN: 1573-4919
    Schlagwort(e): hexokinase degradation ; reticulocyte maturation ; Ca2+ ; SHAM
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract In rabbit reticulocytes more than half of the total hexokinase activity is mitochondrial bound and shows a fast decay during reticulocyte maturation. During in vitro incubation of rabbit reticulocytes, Ca2+ increases the decay of hexokinase while salicylhydroxamate (SHAM), an inhibitor of lipoxygenase, reduces the decay. Swelling of mitochondria, by incubation of the cells in hypotonic solutions, greatly enhances hexokinase decay, but both the Ca2+ and SHAM are still appreciable suggesting that Ca2+ and the swelling act by additive mechanisms, both able to influence hexokinase decay. This was confirmed by incubation of rabbit brain mitochondria in hypotonic solutions which does not promote any hexokinase decay, while the presence of Ca2+ does. Analyses of hexokinase isozymic pattern after incubation of reticulocytes in hypotonic solution both with and without Ca2+ and SHAM showed that the decay of hexokinase mainly involves the mitochrondrial bound isozymic forms.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Springer
    Molecular and cellular biochemistry 79 (1988), S. 133-136 
    ISSN: 1573-4919
    Schlagwort(e): hexokinase heterogeneity ; reticulocyte maturation ; (rabbit)
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie , Chemie und Pharmazie , Medizin
    Notizen: Abstract Hexokinase in rabbit reticulocytes is present in two molecular forms (hexokinase Ia and Ib) separable by ion-exchange chromatography on DE-52 columns. By the use of ion-exchange HPLC we have been able to show that the isozymic form we previously called hexokinase la can be resolved into two peaks of activity one of which is (Ia) soluble, the other (Ia*) particulate. Hexokinase Ia* can be solubilized by detergents like saponine and Triton X-100 and disappears during ‘in vivo’ reticulocytes maturation. This new hexokinase micro-heterogeneity is not caused by different oxidized forms of the enzyme nor influenced by the presence of proteolytic inhibitors during lysate preparation.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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