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  • Yeast  (3)
  • Mercaptoethanol  (1)
  • 1990-1994  (4)
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  • 1
    Digitale Medien
    Digitale Medien
    Purification and some properties of membrane-bound and soluble pyrophosphatases of yeast vacuolesThis paper is dedicated to the memory of the late Prof. N. van Uden. (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 805-812 
    Details
    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
    URL: http://dx.doi.org/10.1002/yea.320070805
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Digitale Medien
    Digitale Medien
    Change in transport activities of vacuoles of the yeast Yarrowia lipolytica during its growth on glucose (1993)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 9 (1993), S. 121-126 
    Details
    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
    URL: http://dx.doi.org/10.1002/yea.320090203
    Standort Signatur Erwartet Verfügbarkeit
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  • 3
    Digitale Medien
    Digitale Medien
    Transport of organic acid anions and guanosine into vacuoles of Saccharomyces pastorianus (1991)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 7 (1991), S. 495-501 
    Details
    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
    URL: http://dx.doi.org/10.1002/yea.320070509
    Standort Signatur Erwartet Verfügbarkeit
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  • 4
    Digitale Medien
    Digitale Medien
    Mercaptoethanol and dithiothreitol decrease the difference of electrochemical proton potentials across the yeast plasma and vacuoar membranes and activate their H+-ATPases (1992)
    New York, NY [u.a.] : Wiley-Blackwell
    Yeast 8 (1992), S. 589-598 
    Details
    ISSN: 0749-503X
    Schlagwort(e): Mercaptoethanol ; dithiothreitol ; plasmalemma ; tonoplast ; H+-ATPase ; H+-permeability ; yeast ; Life and Medical Sciences ; Genetics
    Quelle: Wiley InterScience Backfile Collection 1832-2000
    Thema: Biologie
    Notizen: Mercaptoethanol and dithiothreitol (DTT) inhibited the acidification of external medium by by Saccharomyces Carlsbergensis cells and protoplasts during glucose oxidation. The inhibition was also observed when cells were incubated with mercaptoethanol or when mercaptoethanol and DTT were used to prepare protolasts. Experiments with S. carlsbergensis plasma membrene vesicles and vacuoles showed these thiol reagents to inhibitATP-dipendent generation of ΔpH and Em across plasma membrane vesicles and vacuoles but to activate their H+-ATPases. Mercaptoethanol and DTT are suggested to de-energize plasmalemma as well as tonoplast by increasing their H+-permeability and to disturb the cell ion homeostasis.
    Zusätzliches Material: 4 Ill.
    Materialart: Digitale Medien
    URL: http://dx.doi.org/10.1002/yea.320080803
    Standort Signatur Erwartet Verfügbarkeit
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