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1984 (2)
1979 (1)
1Author    N. Ald, J. Scales, StefanR H IghsmRequires cookie*
 Abstract    lec tr o n M ic r o sc o p ic E vid en ce fo r th e T ran sm em b ran e D isp la ce m e n t o f C alcium A T P a se Incubation o f the Ca2+-ATPase in vanadate solutions leads to the formation o f two-dim ensional arrays in the sarcoplasmic reticulum membrane. Electron micrographic freeze fracture replicas show depressions on the inner leaflet for the first time. This indicates that the ATPase has moved perpendicular to the plane o f the m embrane. Our results also suggest that aggregation o f the Ca2+-ATPase into the two-dim ensional arrays occurs before they move into the membrane. These phenom ena were observed as soon as 15 minutes after vanadate was added. The effects o f vanadate appear to be com pletely reversible. When SR was incubated in the vanadate solutions and was then diluted into a buffer containing Ca2+ and ATP, the ATPase activity was normal for up to several hours o f incubation and only somewhat reduced after 3 days. 
  Reference    Z. Naturforsch. 39c, 177 (1984); received May 30/Septem ber 29 1983 
  Published    1984 
  Keywords    Sarcoplasmic Reticulum, Ca2+-ATPase, Ion Transport, Vanadate 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0177_n.pdf 
 Identifier    ZNC-1984-39c-0177_n 
 Volume    39 
2Author    A. Hager, W. BiberRequires cookie*
 Title    Functional and Regulatory Properties of H + Pumps at the Tonoplast and Plasma Membranes of Zea mays Coleoptiles  
 Abstract    A microsomal membrane fraction (6000 x g supernatant of a cell homogenate), isolated from coleoptiles of Zea mays, was separated by isopycnic sucrose density gradient centrifugation in the presence of EDTA and without a prior pelleting step to avoid irreversible sticking of different membrane species. The membrane fractions were characterized by assaying commonly used marker enzymes, and the levels of activity investigated of ATP hydrolysis, ATP-dependent H+ transport, and co-and countertransport o f ions, such as Cl-, fumarate2-, K+ and Li+. The following results were obtained: 
  Reference    Z. Naturforsch. 39c, 927—937 (1984); received August 6 1984 
  Published    1984 
  Keywords    ATPase, H+-Pumping, Ion Transport, Coleoptile, Zea mays 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0927.pdf 
 Identifier    ZNC-1984-39c-0927 
 Volume    39 
3Author    G. Kliinger, E. BrodaRequires cookie*
 Title    Der Einfluß zweiwertiger Fremdkationen auf die Aufnahme von Zink durch Chlorella Influence o f Twovalent Foreign Cations on the Uptake of Zinc by Chlorella  
 Abstract    The influence o f 10-4 divalent cations on the uptake o f labelled Zn in the concentration range 10~5 to 5 x 10-5 M into the interior o f Chlorella fusca at 30 °C was measured during 75 min. The Zn adsorbed on the surface or contained in the free space was rem oved by washing with EDTA. Corrections were applied for the loss in concentration due to surface adsorption, etc. The results were consistent with com petitive inhibition o f Zn uptake by the foreign ions. N o allosteric inh ib i­ tion was found. From the Lineweaver-Burk diagram, for uninhibited Zn, Ä^M was found as 7 x 1 0 "® M and vmax as 8.3 x lO -9 mol • m in_1-g -1 algae. The inhibitor constants were: Mg 1.3 xlO -5, Ca 4.3 x 10~5, Co 4.3 x 10-5, N i 4.3 x 10~5, Cd 1.3 x 10~5 and Pb 9.4 x 10~7 m. The values given for K m and the inhibitor constant refer to the velocities o f uptake after 45 min. 
  Reference    Z. Naturforsch. 34c, 751—756 (1979); eingegangen am 15. Juni 1979 
  Published    1979 
  Keywords    Chlorella, Green A lgae, Zn M etabolism, Ion Transport, Ion Com petition 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0751.pdf 
 Identifier    ZNC-1979-34c-0751 
 Volume    34