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1987 (1)
1Author    G. Ünter Schmidt, PeterG. RäberRequires cookie*
 Title    The Rate of ATP Hydrolysis Catalyzed by Reconstituted CF0F i-Liposomes  
 Abstract    The conditions for optimal rates of ATP hydrolysis catalyzed by the chloroplast ATP-synthase (A T P ase), CFoF,, after isolation and reconstitution into asolectin liposomes have been investi­ gated. The rate of ATP hydrolysis was m easured either after oxidation of CF0F, (by incubation with iodosobenzoate) or after reduction of CFoF, (by incubation with dithiothreitol). In both cases a rate of about 1 -2 A TP (CF0F i-s)" ' was observed under uncoupled conditions. If the pro-teoliposom es are first energized by an acid-base transition and a K"/valinomycin diffusion po ten ­ tial, the uncoupled rate of A TP hydrolysis is about 1 -2 A TP (CFnF, -s) '1 for the oxidized enzyme and about 20 for the reduced species. This rate is about a factor 2 smaller than that observed in chloroolasts under the same conditions. 
  Reference    Z. Naturforsch. 42c, 231 (1987); received O ctober 17 1986 
  Published    1987 
  Keywords    A TP Hydrolysis, ATP Synthase, A TPase, Reconstitution, CF0F, Liposomes 
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 TEI-XML for    default:Reihe_C/42/ZNC-1987-42c-0231.pdf 
 Identifier    ZNC-1987-42c-0231 
 Volume    42