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1Author    G. Ünther, F. E. SchererRequires cookie*
 Title    A New M ethod to Prepare M em brane F ractions Containing Ionophore-Stim ulated A T P a se from Pumpkin H ypocotyls (Cucurbita maxima, L .)  
 Abstract    In membrane fractions from pumpkin hypocotyls AT­ Pase activity was stimulated by a combination o f CCCP (carbonyl cyanide m-chlorophenylhydrazone), a pro-tonophore, and valinomycin, a K +-ionophore. Singly, these ionophores stimulated ATPase activity much less. Nigericin, an H+/K +-antiporter, and nystatin, a cation pore, had similar effects as the combination o f CCCP and valinomycin. The results suggest the presence o f a cation-translocating ATPase which is stimulated by ionophores by dissipating cation gradients formed in the vesicles. A major part of the ionophore-stimulated ATPase activity correlat­ ed with marker enzymes for plasma membranes but part o f it could be located in other compartments. 
  Reference    Z. Naturforsch. 37c, 550 (1982); received March 5 1982 
  Published    1982 
  Keywords    H +-ATPase, Ionophores, Plasma Membrane, Cucurbita 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0550_n.pdf 
 Identifier    ZNC-1982-37c-0550_n 
 Volume    37 
2Author    BodoC., TagRequires cookie*
 Title    Specific Crystal Chemical Interactions between Carcinogenic Aromatic Compounds and Cholesterol  
 Abstract    Polycyclic aromatic hydrocarbons and aromatic amines exercise a highly specific influence on the crystallization o f cholesterol. The strength o f these non-covalent, presumably epitaxial interactions correlates with the carcinogenic activity o f these substances. The presented results are in support o f the assumption that a specific process o f adsorption and crystallization with cholesterol o f the plasma membrane takes place during the initial phase o f the carcinogenesis by aromatic compounds. 
  Reference    Z. Naturforsch. 46c, 663—6 (1991); received September 6 1988/March 21 1991 
  Published    1991 
  Keywords    Carcinogenic Aromatic Compounds, Epitaxial Adsorption, Cholesterol, Plasma Membrane 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0663.pdf 
 Identifier    ZNC-1991-46c-0663 
 Volume    46 
3Author    Michaela Dane, Kerstin Steinert, Kordula Esser, Susanne Bickel-Sandkötter, Francisco Rodriguez-ValeraRequires cookie*
 Title    Properties of the Plasma Membrane ATPases of the Halophilic Archaebacteria Haloferax mediterranei and Haloferax volcanii  
 Abstract    Both, Haloferax mediterranei and Haloferax volcanii membranes contain ATPases which are capable of hydrolyzing ATP in presence of Mg2+ or M n2+. The ATPases require high con­ centrations of NaCl, a pH value of 9, and high temperatures up to 60 °C. Free manganese ions inhibited the enzyme activity of either ATPase. The ATPases of H f. mediterranei and H f. vol­ canii, respectively, show different sensitivities to inhibitors of ATP hydrolysis. ATP hydrolysis of isolated H f. mediterranei ATPase was inhibited by N aN 3, which was reported to be specific for F-ATPases, by nitrate and N-ethylmaleimide (NEM), which are specific inhibitors of V-ATPases. ATP hydrolysis of H aloferax mediterranei membranes was not inhibited by DCCD , but [14C]DCCD was bound to a 14 kDa peptide of the isolated, partially purified en­ zyme. Furthermore, the ATPase was inactivated by preincubation with 7-chloro-4-nitro-benzofurazan (NBD-C1). The ATPase activity of H f. volcanii membranes was inhibited by NEM but not by nitrate and N aN 3. SDS gel electrophoresis of the partially purified enzyme of Haloferax mediterranei showed putative ATPase subunits of 53. and 7.5 kDa. Immunoblots showed cross reactivity between a 53 kDa peptide and anti-$ (chloro­ plast F(), as well as between 53, 50 and 47 kDa peptides and an ATPase antibody of Methano-sarcina barkeri. The results will be discussed in context with the placement of the archaebac-terial ATPases (A-ATPases) between F-and V-ATPases. 
  Reference    Z. Naturforsch. 47c, 835—844 (1992); received June 29/September 10 1992 
  Published    1992 
  Keywords    Archaebacteria, Plasma Membrane, ATPase, Subunits, ATP Hydrolysis, Inhibition 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0835.pdf 
 Identifier    ZNC-1992-47c-0835 
 Volume    47 
4Author    RichardT C HuangRequires cookie*
 Title    Labeling of Animal Cells with Fluorescent Dansyl Cerebroside  
 Abstract    A dansyl (diaminonaphthalenesulfonyl)-derivative of cerebroside was prepared which could be effectively incorporated into the plasma membranes of tissue culture cells and erythrocytes. The cells which had assimilated the glycolipid fluoresced intensely and could be observed under a fluorescent microscope. Cells were initially labeled rather homogeneously over the whole surface. With longer incubation time organization of the fluorescent glycolipid took place and patches of the lipid in the membrane were formed. The redistribution and organization of the membrane lipid could be demonstrated most clearly when cells labeled with this fluorescent glycolipid were infected with myxoviruses. After infection of MDBK and BHK cells with fowl plague virus areas of dense fluorescence appeared at margines of neighboring cells. When BHK cells were infected with Newcastle disease virus fusion of the cells was accompanied by complete redistribution of the glycolipid. Erythrocytes could also easily incorporate dansyl cerebroside. Chicken erythrocytes which contain cytoplasmic and nuclear membranes incorporated the fluorescent glycolipid in both mem­ branes. T n t v n iliic t io Q 
  Reference    (Z. Naturforsch. 31c, 737 [1976]; received September 9 1976) 
  Published    1976 
  Keywords    Fluorescence Labeling, Dansyl Glycolipids, Glycolipid Patches, Plasma Membrane, Myxoviruses 
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 TEI-XML for    default:Reihe_C/31/ZNC-1976-31c-0737.pdf 
 Identifier    ZNC-1976-31c-0737 
 Volume    31 
5Author    RichardT C HuangRequires cookie*
 Title    Transfer of Glycolipid between Membranes of Tissue Culture Cells, Using Dansylcerebroside as a Model  
 Abstract    Donor cells, which had incorporated dansylcerebroside in their membranes, could further transfer this glycolipid to monolayers of acceptor cells. The ease of transfer varied among acceptor cells, BHK cells being the best and MDBK cells the poorest acceptors of the cells tested. The process of transfer seemed to be mediated by lipids rather than by proteins of the mem­ branes. The mode of attachment between donors and acceptors, such as classified as loose contact, tight adhesion or binding by lectin, did not significantly influence the extent of glycolipid transfer. However, modification of plasma membranes by infection of acceptor cells with myxoviruses re­ sulted in enhancement of glycolipid transfer in some cases. Various factors have been evaluated with respect to dynamics of cellular membranes. 
  Reference    (Z. Naturforsch. 32c, 379 [1977]; received January 12/February 2 1977) 
  Published    1977 
  Keywords    Fluorescence Labeling, Dansylcerebroside, Plasma Membrane, Glycolipid Transfer, Tissue Culture Cells 
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 TEI-XML for    default:Reihe_C/32/ZNC-1977-32c-0379.pdf 
 Identifier    ZNC-1977-32c-0379 
 Volume    32 
6Author    ThomasBarbara Kirsch, Helmut Rojahn, KindiRequires cookie*
 Title    Diphosphatase Related to Lipid Metabolism and Gluconeogenesis in Cucumber Cotyledons: Localization in Plasma Membrane and Etioplasts but not in Glyoxysomes  
 Abstract    Diphosphatase (inorganic pyrophosphatase) activity was localized within compartments of cotyledons of germinating cucumber seeds during the stage of maximal conversion of fat into carbohydrates. At this stage, almost 2 mol pyrophosphate are produced during the formation of one mole sucrose from 0.28 mol triglyceride. When organelles of the 2000 x g pellet or 10,000 x g pellet were separated by density gradient centrifugation and gradient flotation, the diphosphatase activity paralleled the profiles of markers of the plastid stroma but was virtually absent from the glyoxysomes. Within the fraction of small vesicles and membranes, diphosphatase was attributed to the plasma membrane. The main portion of diphosphatase, contained in the plastids, was partially purified by chromatography on anion exchange resin and molecular sieving, leading to a 75-fold enrichment compared to the stroma fraction. Trace amounts of diphosphatase observed in the glyoxysomal fraction were analyzed in the same way. Comparison of the isoelectric points and the activity profile at different pH values and the inhibitory effect of the various cations indicated that the trace amounts of diphosphatase activity in the glyoxysome fraction represented contaminations originating from the plastids. The plasma membrane form of diphosphatase is an integral membrane protein which was solubilized with octylglucoside. It was shown to differ from the plastid form in pH optimum and sensitivity towards bivalent cations. All forms of diphosphatase were clearly distinguished from other phosphohydrolytic activities. 
  Reference    Z. Naturforsch. 44c, 937 (1989); received June 7/July 25 1989 
  Published    1989 
  Keywords    Plastid, Plasma Membrane, Glyoxysome, Diphosphatase (Pyrophosphatase), Cucumber Mobilization 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0937.pdf 
 Identifier    ZNC-1989-44c-0937 
 Volume    44 
7Author    S. Mazzuca, L. SportelliRequires cookie*
 Title    Thermal Behaviour of Lymphocyte Membrane: ESR Investigation  
 Abstract    The order parameter, S, of the plasma membrane of in toto human peripheral blood lym­ phocytes was obtained by electron spin resonance spectroscopy in the temperature range 25-41 C. This membrane is completely in the liquid crystalline state above 31 C. In presence of the antigen ETB from Staphylococcus aureus at the concentration of 4 (ig/3 * 107 cells an overall decrease of the order parameter for this membrane is observed. The decrease of 5 is followed by an upwards shift at about 35 C of the temperature of the liquid crystalline state. 
  Reference    Z. Naturforsch. 45c, 1060—1062 (1990); received April 6 1990 
  Published    1990 
  Keywords    Plasma Membrane, Lymphocyte, Phase Transition, Staphylococcal Enterotoxin B, Spin Labeling 
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 TEI-XML for    default:Reihe_C/45/ZNC-1990-45c-1060.pdf 
 Identifier    ZNC-1990-45c-1060 
 Volume    45 
8Author    Z. NaturforschRequires cookie*
 Title    Lipoxygenase Forms Located at the Plant Plasma Membrane  
 Abstract    In cucumber cotyledons (Cucumis sativus L.) containing several soluble and particulate forms of lipoxygenase (LOX), the location of LOX forms in microsomes has been studied. We concentrated on the question whether the plasma membrane contains one or more forms of LOX. As methodology, we applied both the two-phase partition with polyethylene glycol/ dextran and density gradient flotation of plasma membrane-enriched membrane fractions. Both methods show that a high percentage of the microsomal LOX can be attributed to the plasma membrane. Emphasis was put on the findings that the LOX located at the plasma membrane consisted of a species behaving as an integral membrane protein and another form characterized as a peripheral membrane protein by solubilization with carbonate. With long distance SDS-PAGE and immunodecoration using anti-lipid body LOX antiserum, it is possible to distinguish between microsomal LOX forms by small but significant differences in size. Treatment of seedlings with methyl jasmonate led to an enhanced level of LOX at the plasma membrane. 
  Reference    Z. Naturforsch. 50c, 29 (1995); received August 29/September 301994 
  Published    1995 
  Keywords    Cucumis (Germination), Integral Membrane Protein, Isoenzyme (Lipoxygenase), Lipoxygenase, Methyl Jasmonate, Plasma Membrane 
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 TEI-XML for    default:Reihe_C/50/ZNC-1995-50c-0029.pdf 
 Identifier    ZNC-1995-50c-0029 
 Volume    50