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1Author    HansWerner Miiller, Margareta BaltscheffskyRequires cookie*
 Title    On the Oligomycin-Sensitivity and Subunit Composition of the ATPase Complex from Rhodospirillum rubrum  
 Abstract    Two alternative procedures for isolation of the oligomycin-sensitive ATPase complex (E. C. 3.6.1.3) from R. rubrum chromatophores are compared with respect to ease, rapidity, and yield. The inhibitory effect of oligomycin on the membrane-bound Ca2+ -ATPase activity is increased during storage of the chromatophores, whereas the effect of oligomycin on the membrane-bound Mg2+ -ATPase activity does not change within a week. Oligomycin-sensitivity of the solubilized ATPase complex depends on the isolation procedure. The enzyme complex consists of at least nine different polypeptides with the apparent molec­ ular weights of (. The polypeptides 2 — 4, 7, and 8 represent subunits of coupling factor 1. 
  Reference    Z. Naturforsch. 34c, 229 (1979); received January 4 1979 
  Published    1979 
  Keywords    Rhodospirillum rubrum, ATPase, Subunits, Oligomycin 
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 TEI-XML for    default:Reihe_C/34/ZNC-1979-34c-0229.pdf 
 Identifier    ZNC-1979-34c-0229 
 Volume    34 
2Author    Hans Liidi, Bernhard Rauch, Wilhelm HasselbachRequires cookie*
 Title    The Influence of Detergents on the Ca2+-and Mg2+-Dependent Adenosine Triphosphatase of the Sarcoplasmic Reticulum  
 Abstract    During the stepwise solubilization of sarcoplasmic reticulum vesicles with detergents, the following changes in the structural and enzymatic properties of the preparation are observed: 1. The viscosity of the vesicular suspension initially rises. This change is accompanied by the formation of elongated tubules. Subsequently the membranes are completely desintegrated, resulting in a considerable reduction of the viscosity. 2. A decrease in the activity of the Ca2+-dependent ATPase, which is restored after complete solubilization. 3. A decrease in the change of intrinsic tryptophan-fluorescence on removal of calcium ions, which is also restored after complete solubilization. 4. A decrease of the calcium affinity of the ATPase. 5. A decrease in the amount of phosphorylated protein formed by the incorporation of inorganic phosphate. On the other hand, the amount of phosphoprotein formed from ATP is not affected during solubilization. 6. The dependence of the initial rates of phosphoprotein formation from inorganic phosphate on either magnesium or inorganic phosphate at low concentrations of the respective ligand changes from an S-shape profile to a normal hyperbolic profile after solubilization. 
  Reference    Z. Naturforsch. 37c, 299—307 (1982); received January 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum, ATPase, Detergent, Protein-Phosphorylation, Kinetics 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0299.pdf 
 Identifier    ZNC-1982-37c-0299 
 Volume    37 
3Author    G. Inesi, M. Kurzmack, D. Kosk-Kosicka, D. Lewis, H. Scofano, H. G. Uim Araes-MottaRequires cookie*
 Title    Equilibrium and Kinetic Studies of Calcium Transport and ATPase Activity in Sarcoplasmic Reticulum  
 Abstract    A number o f equilibrium and kinetic m easurem ents are presented to characterize the partial reactions o f the ATPase and transport cycle in sarcoplasm ic reticulum vesicles. The cycle begins with calcium and nucleotide binding on sites available on the outer surface o f the vesicles. A phosphorylated enzyme intermediate is then formed, and the calcium sites are subjected to a change in their orientation and their affinity for calcium . It is shown that steps involved in cal­ cium release on the inner side o f the vesicles are rate lim iting for the cycle, and are follow ed by hydrolytic cleavage o f the intermediate with release o f inorganic phosphate and recycling o f the enzyme. 
  Reference    Z. Naturforsch. 37c, 685 (1982); received February 6 /M arch 23 1982 
  Published    1982 
  Keywords    Calcium, Transport, ATPase, Sarcoplasm ic Reticulum 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0685.pdf 
 Identifier    ZNC-1982-37c-0685 
 Volume    37 
4Author    Bernhard HuchzermeyerRequires cookie*
 Title    Phosphate Binding to Isolated Chloroplast Coupling Factor (CF^  
 Abstract    A single binding site for phosphate was found on isolated chloroplast coupling factor in the absence of nucleotides. In our experiments the phosphate binding site showed a K d of 170 JIM. We did not observe any differences whether the ATPase activity of CF] had been activated or not. If the enzyme was incubated with [y-32 P]ATP the amount of 32 P bound per CF, depended on the pretreatment of the enzyme: In the presence of ADP no ATP or phosphate was bound to CF,. After activation of ATPase activity one mol of ATP per mol CF, was rapidly bound and hydro-lyzed while there was a slowly occurring binding of another phosphate without concomitant nucleotide binding. We conclude that there are two different types of phosphate binding observed in our experi-ments: 1) Inorganic phosphate can be bound by one catalytic site per mol of CTv 2) The y-phosphate of ATP is able to bind to an ATP binding domain of the enzyme if this domain can exchange substrates with the incubation medium. This ATP binding domain appears to differ from the site binding inorganic phosphate, because at least a portion of the coupling factor contains more than one labelled phosphate during our ATPase tests. 
  Reference    Z. Naturforsch. 43c, 213—218 (1988); received July 27/November 19 1987 
  Published    1988 
  Keywords    Chloroplast, Coupling Factor, Binding Sites, ATPase, Phosphorylation 
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 TEI-XML for    default:Reihe_C/43/ZNC-1988-43c-0213.pdf 
 Identifier    ZNC-1988-43c-0213 
 Volume    43 
5Author    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 
6Author    Wolfgang Lockau, Susanne PfefferRequires cookie*
 Title    A Cyanobacterial ATPase Distinct from the Coupling Factor of Photophosphorylation  
 Abstract    A particle-bound, M g2+-dependent A TPase activity is investigated in cell-free extracts o f the cyanobacterium Anabaena variabilis. The enzym e can be clearly distinguished from the 
  Reference    Z. Naturforsch. 37c, 658 (1982); received March 231982 
  Published    1982 
  Keywords    Cyanobacterium, Anabaena variabilis, ATPase, Coupling Factor, Cytochrom e Oxidase 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-0658.pdf 
 Identifier    ZNC-1982-37c-0658 
 Volume    37 
7Author    Hans Liidi, Wilhelm HasselbachRequires cookie*
 Title    Fluorescence Studies on N-(3-Pyrene)Maleinimide-Labeled Sarcoplasmic Reticulum ATPase in Native and Solubilized Membranes  
 Abstract    Fluorescence polarization and formation of excimers were studied in N-(3-pyrene)malein-imide-labeled sarcoplasmic reticulum vesicles. 1. The polarization of pyrenemaleinimide labeled vesicles does not change with temperature and shows a pronounced decrease at labeling concentrations larger than 1 mol pyrenemaleinimide per 10 mol ATPase. 2. Solubilization of the membrane with myristoylglycerophosphocholine renders the polariza­ tion temperature dependent, but does not affect the concentration dependent depolarization observed in native vesicles. 3. The polarization of labeled vesicles is much smaller than to be expected from the tempera­ ture independent polarization indicating that the pyrenemaleinimide polarization did not monitor the rotation of the entire ATPase. Thus segmental motion occurs. 4. Pyrene excimers are observed at label concentrations larger than 1 mol label per 2.5 mol ATPase. 5. The amount of excimers was critically dependent on added detergents. From the fact that non-solubilizing amounts of myristoylglycerophosphocholine strongly reduced the amount of pyrene excimers it is concluded that in the native sarcoplasmic reticulum vesicles at least two ATPase molecules must be in close contact. 
  Reference    Z. Naturforsch. 37c, 1170 (1982); received August 16 1982 
  Published    1982 
  Keywords    Sarcoplasmic Reticulum, ATPase, Protein-Protein-Interactions, Fluorescence Polarization, Excimer Formation 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-1170.pdf 
 Identifier    ZNC-1982-37c-1170 
 Volume    37 
8Author    Hector Barrabin, Leopoldo De MeisRequires cookie*
 Title    Phosphorylation of Ca-ATPase of Sarcoplasmic Reticulum with Different Substrates  
 Abstract    ATP and G TP as substrate for phosphorylation o f sarcoplasm ic reticulum A TPase are compared. Maximal levels o f phosphoenzyme are between 4.5 and 4.8 nmol per mg o f protein when either substrate is used provided that phosphoenzym e hydrolysis are strongly inhibited by high calcium concentration (20 mM) and low tem peratures (0 ° C) . T he m axim al values obtained with G TP are lower than those previously reported. It is shown that this difference is due to underestim ation o f the specific activity o f labeled nucleotides used in previous studies, as revealed by U V absorption and H PLC analysis. The dependence o f the phosphoenzyme levels on calcium concentration, pH and tem perature confirm previous findings indicating that ATP, but no G T P , accelerates the rate limiting step o f the catalytic cycle. 
  Reference    Z. Naturforsch. 38c, 845 (1983); received M arch 2 4/Ju n e 16 1983 
  Published    1983 
  Keywords    Calcium, ATPase, Sarcoplasm ic Reticulum, H PLC, N ucleotides 
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 TEI-XML for    default:Reihe_C/38/ZNC-1983-38c-0845.pdf 
 Identifier    ZNC-1983-38c-0845 
 Volume    38 
9Author    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 
10Author    Susanne Bickel-Sandkötter, K. Ordula Esser, M. Artina, H. OrbachRequires cookie*
 Title    On the Accessibility of Essential Tyrosines in Isolated and Activated Chloroplast H +-ATPase  
 Abstract    The addition o f 7-chloro-4-nitrobenzofurazan to isolated and activated CF, creates a com ­ pletely changed binding stoichiometry and subunit-distribution o f bound modifier in contrast to the binding pattern in not-activated CF,. The activation o f CF, by dithiothreitol and heat results in the accessibility o f three additional tyrosines in ß-subunits and one additional tyro­ sine in a-subunits. Binding o f pyridoxalphosphate to lysine in the active state suppresses the accessibility o f the additional tyrosines, suggesting that PLP inactivates the ATPase by induc­ ing a conformational change. Furthermore, two N BD -m olecules are bound to y-subunits when CF, is activated. These two molecules may be bound to sulfhydryl groups o f cysteines which become accessible to N B D after activation. 
  Reference    Z. Naturforsch. 46c, 71—78 (1991); received September 7 1990 
  Published    1991 
  Keywords    ATP-Hydrolysis, ATPase, Chloroplast, Covalent M odification, Subunit Labeling 
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 TEI-XML for    default:Reihe_C/46/ZNC-1991-46c-0071.pdf 
 Identifier    ZNC-1991-46c-0071 
 Volume    46 
11Author    ErwinW. BeckerRequires cookie*
 Title    Dynamics and Kinetics of Enzymes Kinetic Equilibrium of Forces in Biochemistry  
 Abstract    To explain the high specificity, high reaction rate, and high thermodynamic efficiency in enzymatic processes, cooperation of the enzyme with a molecular transfer unit is assumed. A "kinetic equilibrium of forces" is suggested, which enables high reaction rates to occur under equilibrium conditions and a thorough examination of the substrate to be made without con­ sumption of free energy. In case o f ATPases, ion-binding proteins are the most probable trans­ fer units. By analyzing the elementary effect in muscle contraction it is shown that the new theorem may be of substantial value in elucidating biochemical processes. 
  Reference    Z. Naturforsch. 47c, 628—633 (1992); received May 18 1992 
  Published    1992 
  Keywords    Enzyme, Mechanism, Free Energy Transfer, ATPase, Calmodulin, Muscle Contraction 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0628.pdf 
 Identifier    ZNC-1992-47c-0628 
 Volume    47 
12Author    Hans-Jochen Schäfer, Gabriele Rathgeber, Klaus Dose, HubertusE. Sauer, WolfgangE. TrommerRequires cookie*
 Title    3'-Arylazido-ß-aIanyI-2-azido ATP, a Cross-Linking Photoaffinity Label for FiATPases  
 Abstract    The synthesis of the 3'-arylazido-2-azido ATP derivative 3'-0-{3-[N-(4-azido-2-nitrophenyl)-amino]propionyl}2-azido-adenosine 5'-triphosphate (2,3'-DiN3ATP) is described. The bifunc­ tional photoreactive ATP analog is characterized spectroscopically. Photoaffinity labeling of F, ATPase from Micrococcus luteus by this analog results in the inactivation of the enzyme and in the formation of higher molecular weight cross-links, 
  Reference    Z. Naturforsch. 44c, 955 (1989); received July 12 1989 
  Published    1989 
  Keywords    Bacterial F, ATPase, Nucleotide Conformation, Photoaffinity Labeling, Catalytic Nucleotide Binding Site, a-ß Interface 
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 TEI-XML for    default:Reihe_C/44/ZNC-1989-44c-0955.pdf 
 Identifier    ZNC-1989-44c-0955 
 Volume    44