Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0268318 (ICP)
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Eight coordinated complex samples of CoCl2-NaDC were obtained,using various concentration and initial molar ratio of CoCl2 and NaDC. They exhibited distinct appearances and characters. Their different structures and components were investigated by FTIR spectroscopy, X-ray diffraction analysis and ICP analysis. We can give the following conclusions: (1) when the concentration of NaDC is smaller than C.M.C, Co2+ ions react with mono-molecular NaDC and the component of the pink wadding-like resultant is Co(DC)2 x 3H2O. (2) When the concentration of NaDC is larger than C.M.C, and the concentration of CoCl2 is higher (0.5 mol/L), Co2+ ions destroy NaDC micelles, and the component of the pink wadding-like resultant is also Co(DC)2 x 3H2O. (3) When the concentration of NaDC is larger than C.M.C, and the concentration of CoCl2 is lower (0.1 mol/L or more lower), Co(DC)2 and NaDC may form mixed micelles, and some of NaDC micelles connect with each other through the Co2+ bridges to produce complicate Co(DC)2-NaDC complex with gel character and macromolecular network structure. In human body,the concentration of metal ions is usually lower and the concentration of NaDC is larger than C.M.C, So the third kind is suggested as an ideal model of the interaction between Co2+ ions and NaDC in vivo.
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PMID:[Study on the Co(DC)2-NaDC mixed micelle system]. 1581 96

Direct interaction of Cu2Zn2SOD with inorganic metal compound (CoCl2) and organic metal compound [Co(II)(His)n] was studied by ICP, VIS, NMR and measurement of enzyme activity. It has been found that in aqueous solution, there exists a direct interaction of the metal ions of the active center in the metalloenzyme (Cu2Zn2SOD) with external added CoCl2, Co(His)n. As a result, part of the metal ions in metalloenzyme were replaced and the corresponding metalloenzyme derivatives were produced and the catalytic activity of enzyme were affected. Moreover, the interaction of Co(II)(His)n with Cu2Zn2SOD is stronger and quicker, than that of CoCl2 with this enzyme, as well as the Co(II) from Co(II)(His)n is easier to enter the active center of enzyme.
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PMID:[Study on the interaction of Cu2Zn2SOD with CoCl2, Co(His)n by spectral and magnetic resonance analysis]. 1581 41