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EN
Thermal decomposition behavior of bis (4-nitrophenol)-2,4,6-triamino-1,3,5-triazine monohydrate (BNPM) has been studied by means of thermogravimetric analysis at three different heating rates 10, 15 and 20°C min¯¹. Non-isothermal studies of BNPM have revealed that the decomposition occurs in three stages involving dehydration and decomposition. The values of effective activation energy (E_{a}), pre-exponential factor (A) of each stage of thermal decomposition for all heating rates were calculated by model free methods: Arrhenius, Flynn-Wall, Friedman, Kissinger and Kim-Park method. A significant variation of effective activation energy (E_{a}) with conversion (α) indicates that the process is kinetically complex. The linear relationship between the A and E_{a} values was well established (compensation effect). Dehydration stage was governed by the Avrami-Erofeev model (A2) and decomposition stages were governed by the Avrami-Erofeev model (A4).
EN
The purpose of this study is synthesis, characterization and enzyme activity functions of novel dinuclear metal complexes. Therefore two new dinuclear heterometallic cobat(II)-copper(II) complexes have been synthesized and structurally characterized by using Fourier transform infrared method, elemental analysis, inductively coupled plasma optical emission spectrometry, molar conductivity, magnetic moment measurements and thermal analysis. Spectroscopic and stoichiometric data of the metal complexes indicated that the metal:ligand ratio of the complexes were found to be 2:1. Both of the complexes are 1:2 electrolytes as shown by their molar conductivities and paramagnetism. The subnormal magnetic moment values of the dinuclear complexes were explained by an antiferromagnetic interaction. Additionally complexes were each tested both for their ability to oxidation reaction of 3,5-di-tert-butylcatechol to the 3,5-di-tert-butyl-o-benzoquinone presence of O₂ and catalyse the disproportionation of hydrogen peroxide in the presence of the added base imidazole. It was found that both of the complexes exhibited good catecholase and catalase-like enzyme activity.
EN
One of the main questions regarding protein adsorption is about the reversibility of the adsorption process. To get a deeper understanding of this, adsorption of ferritin on Au was studied by quartz crystal microbalance and the pH of the buffer was changed in situ between two values that favour adsorption by different amounts. We found that although some ferritin desorbs from Au, the desorption is incomplete. When the desorption reached a constant value, we returned to the original conditions and investigated the readsorption. Our experiments show that the adsorption of ferritin onto Au is a partly reversible process. We found that for different initial ferritin coverages the proportion of ferritin that had been subsequently desorbed was approximately constant.
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