ALBERT

All Library Books, journals and Electronic Records Telegrafenberg

feed icon rss

Ihre E-Mail wurde erfolgreich gesendet. Bitte prüfen Sie Ihren Maileingang.

Leider ist ein Fehler beim E-Mail-Versand aufgetreten. Bitte versuchen Sie es erneut.

Vorgang fortführen?

Exportieren
Filter
  • Artikel  (4)
  • Yeast  (4)
  • vacuole  (2)
Sammlung
  • Artikel  (4)
Verlag/Herausgeber
Erscheinungszeitraum
Thema
  • 1
    ISSN: 1432-072X
    Schlagwort(e): Ions ; Concentration ; Regulation ; Cytoplasm ; Vacuole ; Yeast ; Saccharomyces carlsbergensis
    Quelle: Springer Online Journal Archives 1860-2000
    Thema: Biologie
    Notizen: Abstract Intracellular distributions of K+, Mg2+ and orthophosphate under various conditions of cultivation or incubation of the yeast Saccharomyces carlsbergensis were studied by differential extraction of ion pools. The decisive role of vacuolar compartmentation of ions in regulation of K+, Mg2+ and orthophosphate levels in the yeast cytoplasm was shown. The content of intracellular K+ and Mg2+ in yeast increased or decreased primarily depending on the increase or decrease in the vacuolar ion pool. The levels of K+ and Mg2+ in the cytoplasm were practically unchanged. Vacuoles were involved in regulation of Mn2+ concentration in the cytoplasm of the yeast S. carlsbergensis accumulating this ion in the presence of glucose. Alongside the vacuolar compartmentation, the chemical compartmentation, i. e. formation of bound Mg2+, Mn2+ and K+ was, evidently, also involved in the control of ion levels in the cytoplasm. The orthophosphate level in the yeast cytoplasm was regulated by its accumulation in vacuoles and biosynthesis of inorganic polyphosphates in these organelles. The biosynthesis of low-molecular weight polyphosphates occurred parallel to the accumulation of Mg2+ or Mn2+ in vacuoles, thus confirming the availability of the other mechanism for the transport of these ions through the tonoplast differing from the transport mechanism through the plasmalemma.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 2
    Digitale Medien
    Digitale Medien
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 495-501 
    ISSN: 0749-503X
    Schlagwort(e): Yeast ; vacuole ; H+-ATPase ; guanosine ; organic acids transport ; Ca2+-modulation ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: Isolated vacuoles of the yeast Saccharomyces pastorianus accumulate citrate, α-ketoglutarate, malate and guanosine. This accumulation is Mg ATP-dependent and inhibited by protonophores. The ionophores monensin and A23187 (electroneutral Men+/nH+-exchange) inhibit guanosine accumulation but fail to block citrate uptake. Mg2+ ions (2 mM) increase the values of both Δ\documentclass{article}\pagestyle{empty}\begin{document}$ \tilde \mu $\end{document}H+ components and stimulate the uptake of all the above compounds. Ca2+ ions (1 mM), hyperpolarizing the yeast vacuolar membrane and dissipating the pH gradient, inhibit guanosine uptake and stimulate that of citrate. It is concluded that guanosine is transported into yeast vacuoles by an H+/guanosine antiporter while citrate, malate and α-ketoglutarate are translocated by a uniporter(s) at the expense of the membrane potential (positive inside).
    Zusätzliches Material: 7 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 3
    ISSN: 0749-503X
    Schlagwort(e): Yeast ; vacuoles ; pyrophosphatase ; H+-transport ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: The membrane-bound and soluble pyrophosphatase (PPase) activities of Saccharomyces carlsbergenis vacuoles are determined by the functioning of special enzymes and are not due to non-specific PPi hydrolysis by other vacuolar phosphohydrolases. The molecular mass of the membrane-bound PPase is apparently 120 000 and its molecule consists of three subunits with Mr = 41 000. Soluble PPase has a molecular mass of about 82 000 and includes three subunits with Mr = 28 000. Both enzymes are glycoproteins. The vacuolar membrane-bound PPase is a proton pump.
    Zusätzliches Material: 8 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
  • 4
    ISSN: 0749-503X
    Schlagwort(e): Yeast ; vacuole ; H+-ATPase ; citrate transport ; ΔpH ; membrane potential ; growth phase ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: Vacuoles were isolated from Yarrowia lipolytica yeast cells taken at various growth phases under carbon or nitrogen limitation. Vacuoles from the cells at the logarithmic growth phase showed a high activity of vacuolar H+-ATPase (0·9-1·1 U/mg protein) and efficiently generated chemical proton gradient and membrane potential across the tonoplast. Ca2+- and citrate transport were found to be maximal at this growth phase. At growth retardation and then in the stationary phase all the parameters studied decreased irrespective of the method of growth limitation. The citrate-transporting activity of vacuoles completely disappeared at growth retardation, also irrespective of the limitation method and irrespective of whether yeast cells overproduced citrate in the culture medium. The citrate-transporting system of Y. lipolytica vacuolar membrane is concluded not to be involved in citrate efflux and this efflux is probably performed by the plasmalemma transport system.
    Zusätzliches Material: 3 Ill.
    Materialart: Digitale Medien
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
Schließen ⊗
Diese Webseite nutzt Cookies und das Analyse-Tool Matomo. Weitere Informationen finden Sie hier...