123952-70-5Relevant articles and documents
Oxidation of putrescine and cadaverine derivatives by diamine oxidases
Equi, Angela M.,Brown, Alison M.,Cooper, Alan,Her, Surjit K.,Watson, Allan B.,Robins, David J.
, p. 507 - 518 (1991)
A range of putrescine and cadaverine derivatives has been synthesized and assayed as substrates for the diamine oxidases from pea seedlings and pig kidney. KM and Vmax data are reported, mainly for the pea enzyme. N-Alkylputrescines and C-alkylcadaverines are generally poorer substrates than the parent compounds with up to 4500-fold reduction in Vmax. There is significantly less variation in KM values, indicating that the binding site of the pea enzyme is relatively non-specific and that enzymic specificity lies at the catalytic stage. This suggests that poor substrates might act as convenient, short-lived inhibitors of diamine oxidases.
Sequestering agent for uranyl chelation: a new family of CAMS ligands
Leydier, Antoine,Lecerclé, Delphine,Pellet-Rostaing, Stéphane,Favre-Reguillon, Alain,Taran, Frédéric,Lemaire, Marc
, p. 6662 - 6669 (2008/12/20)
The synthesis of new dipodal bis-sulfocatecholamide uranophiles is presented. Their binding abilities for uranyl cation were determined by UV spectrophotometry in aqueous media under various pH conditions and further studied by 1H NMR analysis of the resonance signal of both aromatic protons of the sulfocatecholamide groups. The results showed that the efficiency of these hydrosoluble chelating agents depends on the nature of the spacers. Each ligand shows a more or less pronounced affinity for uranium. The best receptor is the ligand CYCAMS 5d obtained as a mixture of cis/trans isomers, which achieves the best compromise between rigidity and steric hindrance.