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'Enzyme Kinetics' in keywords Facet   section ZfN Section C  [X]
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1992 (1)
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1981 (2)
1Author    Paul RöschRequires cookie*
 Title    Statistical Description of Isotope Exchange Processes: A M ultisite Model for the lsO Exchange  
 Abstract    An analytical procedure has been developed for the determination of isotope exchange processes as exemplified by the l80 exchange catalysed by enzyme-nucleotide complexes. The model is able to handle more than one type of active site per reaction solution and is also able to distinguish between different types of inequivalence of the oxygens of enzyme bound P,. Use of transition matrix formalism and basic statistical considerations lead directly to the simple model. A data refinement procedure is introduced and model calculations are shown. 
  Reference    Z. Naturforsch. 37c, 1161—1169 (1982); received July 15 1982 
  Published    1982 
  Keywords    ATPases, Enzyme Kinetics, l80, Phosphorylation, 3IP-NMR 
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 TEI-XML for    default:Reihe_C/37/ZNC-1982-37c-1161.pdf 
 Identifier    ZNC-1982-37c-1161 
 Volume    37 
2Author    Paul Rösch, HansRobert Kalbitzer, RogerS. GoodyRequires cookie*
 Title    ,sO-Exchange by Hydrolyzing Enzymes: An ab initio Calculation  
 Abstract    Enzymes which hydrolyse ATP cause an exchange of 180 of labelled Pi in the presence of ADP. A theory for the evaluation o f rate constants from an observation o f the time dependence of the concentration o f the various Pi species is presented. Application to the 180 exchange catalysed by myosin SI as observed by 31P-NMR shows excellent agreement with values o f the rate constants determined earlier. 
  Reference    Z. Naturforsch. 36c, 534 (1981); received October 2 1 1980/March 24 1981 
  Published    1981 
  Keywords    180-Exchange, Enzyme Kinetics, 31P-NMR, Myosin SI, Nucleotidases 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0534.pdf 
 Identifier    ZNC-1981-36c-0534 
 Volume    36 
3Author    Paul RöschRequires cookie*
 Title    ,80-Exchange by Hydrolyzing Enzymes: Extension of the Model to Pi Molecules with Inequivalent Oxygen Atoms in the Bound State  
 Abstract    Enzymes causing an exchange o f oxygens from P\ with the surrounding water oxygens are very common. A statistical model for the data evaluation for an observation of this oxygen exchange by isotope methods is presented. It is shown how different cases o f inequivalence o f the four Pi oxygens may be uncovered. The number of reversals o f the oxygen exchange step on the enzyme and the apparent second order rate constant for the binding o f Pi to the enzyme are obtained as a result o f the data fitting procedure. Cobalt phosphatase, zinc phosphatase, and myosin subfragment 1 are treated as examples. 
  Reference    Z. Naturforsch. 36c, 539—544 (1981); received January 28/March 241981 
  Published    1981 
  Keywords    Enzyme Kinetics, ATPases, 31P-NMR, 180-Exchange, Enzyme Mechanism 
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 TEI-XML for    default:Reihe_C/36/ZNC-1981-36c-0539.pdf 
 Identifier    ZNC-1981-36c-0539 
 Volume    36 
4Author    Petra Fromme, Ingo Dahse, PeterG. RäberRequires cookie*
 Title    Effect of Tentoxin on the Activation and on the Catalytic Reaction of Reconstituted H +-ATPase from Chloroplasts  
 Abstract    The proton-translocating ATPase from chloroplasts, C F 0Fj, was isolated, purified and re­ constituted into asolectin liposomes. The effect o f the energy transfer inhibitor, tentoxin, on different functions o f the enzyme was investigated. Tentoxin does not inhibit the nucleotide release during energization by a pH /A T jum p, i.e. the activation o f the enzyme is not influ­ enced. ATP synthesis driven by a pH /A T jump and multi-site ATP hydrolysis are completely inhibited by tentoxin, whereas uni-site ATP hydrolysis is not influenced. 
  Reference    Z. Naturforsch. 47c, 239 (1992); received September 30 1991/January 3 1992 
  Published    1992 
  Keywords    H +-ATPase, CF0F, Tentoxin, Enzyme Kinetics, Uni-Site Catalysis 
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 TEI-XML for    default:Reihe_C/47/ZNC-1992-47c-0239.pdf 
 Identifier    ZNC-1992-47c-0239 
 Volume    47