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1988 (1)
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1Author    G. Csaba, P. Ková, Ágnes Inczefi, -G OndaRequires cookie*
 Title    Insulin B ind ing S ite s Induced in the Tetrahymena by R at Liver R ecep tor A ntibody  
 Abstract    Tetrahvmena cells treated with purified rabbit anti­ bodies to rat hepatocellular membrane exhibited a consider­ able increase in binding capacity on reexposure to the antibody 24 h later. Insulin binding was similarly enhanced by preexposure to the antibody, and vice versa, preex­ posure to insulin enhanced the later binding o f rat liver receptor antibodies. This suggests that (1) the Tetrahymena and the rat possess similar insulin receptors, and (2) the receptor antibody is also able to induce imprinting for itself as well as for insulin. Concanavalin-A, noted for binding overlap with insulin, failed to induce imprinting either for insulin or for antibodies to receptors, whereas the latter did induce imprinting for Concanavalin-A. 
  Reference    Z. Naturforsch. 39c, 183 (1984); received July 4/A ugust 22 1983 
  Published    1984 
  Keywords    Tetrahymena, Receptor-antibody, Insulin, Binding Sites 
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 TEI-XML for    default:Reihe_C/39/ZNC-1984-39c-0183_n.pdf 
 Identifier    ZNC-1984-39c-0183_n 
 Volume    39 
2Author    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 
3Author    Peter Zipper, Helmut DurchschlagRequires cookie*
 Title    Small-Angle X-Ray Scattering on Malate Synthase from Baker's Yeast Considerations on the Effects of Bound Ligands  
  Reference    Z. Naturforsch. 33c, 504 (1978); received June 12 1978 
  Published    1978 
  Keywords    M alate Synthase, Small-Angle X-Ray Scattering, Structural Changes on Ligand Binding, M odels for Enzyme-Substrate Complexes, Binding Site 
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 TEI-XML for    default:Reihe_C/33/ZNC-1978-33c-0504.pdf 
 Identifier    ZNC-1978-33c-0504 
 Volume    33